Scholars@Duke
Celia J. Bonaventura

Celia J. Bonaventura

Professor Emeritus
Marine Science and Conservation
bona@duke.edu
135 Duke Marine Lab Rd, Beaufort, NC 28516

Selected Publications

Molecular controls of the oxygenation and redox reactions of hemoglobin.

Journal Article Antioxidants & redox signaling · June 2013 SignificanceThe broad classes of O(2)-binding proteins known as hemoglobins (Hbs) carry out oxygenation and redox functions that allow organisms with significantly different physiological demands to exist in a wide range of environments. This is a ... Full text Cite

Haptoglobin alters oxygenation and oxidation of hemoglobin and decreases propagation of peroxide-induced oxidative reactions.

Journal Article Free radical biology & medicine · September 2012 We compared oxygenation and anaerobic oxidation reactions of a purified complex of human hemoglobin (Hb) and haptoglobin (Hb-Hp) to those of uncomplexed Hb. Under equilibrium conditions, Hb-Hp exhibited active-site heterogeneity and noncooperative, high-af ... Full text Cite

Steric factors moderate conformational fluidity and contribute to the high proton sensitivity of Root effect hemoglobins.

Journal Article Biochimica et biophysica acta · October 2011 The structural basis of the extreme pH dependence of oxygen binding to Root effect Hbs is a long-standing puzzle in the field of protein chemistry. A previously unappreciated role of steric factors in the Root effect was revealed by a comparison of pH effe ... Full text Cite

Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite.

Journal Article Biochimica et biophysica acta · October 2010 The clam Lucina pectinalis supports its symbiotic bacteria by H₂S transport in the open and accessible heme pocket of Lucina Hb I and by O₂ transport in the narrow and crowded heme pocket of Lucina Hb II. Remarkably, air-equilibrated samples of Lucina Hb I ... Full text Cite

Extreme Differences in Lucina Hemoglobins in their Interactions wtih Nitrite

Journal Article Biochemica Biophysica Acta · March 2010 Cite

Iron in the Oceans (Approximate title)

Journal Article Reference unavailable at this time (Traveling) · July 2008 Problems of iron-induced redox reactions make it likely that adverse reactions can occur upon introduction of iron into marine ecosystems. ... Cite

Oxidative iron species and ocean challenges: a perspective.

Journal Article Biofouling · January 2008 The idea of using oxidative iron (Fe(6+)) to manage fouling and potentially invasive and pathogenic species in ballast water has merit and is attractive when viewed in the broadest context. Ferrate (Fe(6+)) has potential in ballast water management because ... Full text Cite

Genetic diversity of coastal bottlenose dolphins revealed by structurally and functionally diverse hemoglobins.

Journal Article Gene · August 15, 2007 Studies of structure-function relationships in the respiratory proteins of marine mammals revealed unexpected variations in the number and types of hemoglobins (Hbs) present in coastal bottlenose dolphins, Tursiops truncatus. We obtained blood samples from ... Full text Link to item Cite

Allosteric effects on oxidative and nitrosative reactions of cell-free hemoglobins.

Journal Article IUBMB life · August 2007 A review of the oxidative and nitrosative reactions of cell-free hemoglobin-based oxygen carriers (HBOCs) shows that these reactions are intimately linked and are subject to allosteric control. Cross-linking reactions used to produce HBOCs introduce confor ... Full text Cite

Overproduction of alpha chains provides a proton-insensitive component to the bluefish hemoglobin system.

Journal Article J Biol Chem · December 9, 2005 Expression of alpha and beta chains and their post-translational assembly into alpha(2)beta(2) tetramers is fundamental to the formation and function of most vertebrate hemoglobins. There is a strong evolutionary bias that favors expression of equal amount ... Full text Link to item Cite

Critical redox and allosteric aspects of nitric oxide interactions with hemoglobin.

Journal Article Antioxidants & redox signaling · December 2004 Nitric oxide (NO) is an important signaling molecule. Relatively long-lived NO adducts at the heme and SH groups of hemoglobin (Hb) could enable NO to carry out long-range signaling functions. In spite of significant advances, there remain as yet unresolve ... Full text Cite

New insights into the proton-dependent oxygen affinity of Root effect haemoglobins.

Journal Article Acta physiologica Scandinavica · November 2004 A long-standing puzzle with regard to protein structure/function relationships is the proton-dependent modification of haemoglobin (Hb) structure that causes oxygen to be unloaded from Root effect Hbs into the swim bladders and eyes of fish even against hi ... Full text Cite

Domain-specific effector interactions within the central cavity of human adult hemoglobin in solution and in porous sol-gel matrices: evidence for long-range communication pathways.

Journal Article Biochemistry · April 2004 The water-filled central cavity of human adult hemoglobin (Hb A) is the binding or interaction site for many different allosteric effectors. Oxygen binding titrations reveal that pyrenetetrasulfonate (PyTS), a fluorescent analogue of 2,3-diphosphoglycerate ... Full text Cite

The case of the missing NO-hemoglobin: spectral changes suggestive of heme redox reactions reflect changes in NO-heme geometry.

Journal Article Proceedings of the National Academy of Sciences of the United States of America · October 2003 When low levels of gaseous nitric oxide (NO) are equilibrated with deoxygenated Hb, all NO added can be accounted for in terms of hexacoordinate and pentacoordinate forms of NO-Hb, despite recent reports on NO disappearance from heme groups to form nitroxy ... Full text Cite

Functional and biochemical properties of the hemoglobins of the burrowing brittle star Hemipholis elongata say (Echinodermata, Ophiuroidea)

Journal Article Biological Bulletin · 2003 The burrowing brittle star Hemipholis elongata (Say) possesses hemoglobin-containing coelomocytes (RBCs) in its water vascular system. The RBCs, which circulate between the arms and body, are thought to play a role in oxygen transport. The hemoglobin of ad ... Cite

S-Nitrosohemoglobin is unstable in the reductive erythrocyte environment and lacks O2/NO-linked allosteric function.

Journal Article The Journal of biological chemistry · August 2002 Our previous results run counter to the hypothesis that S-nitrosohemoglobin (SNO-Hb) serves as an in vivo reservoir for NO from which NO release is allosterically linked to oxygen release. We show here that SNO-Hb undergoes reductive decomposition in eryth ... Full text Cite

Responses of normal and sickle cell hemoglobin to S-nitroscysteine: implications for therapeutic applications of NO in treatment of sickle cell disease.

Journal Article Biophys Chem · July 10, 2002 Factors which govern transnitrosation reactions between hemoglobin (Hb) and low molecular weight thiols may define the extent to which S-nitrosated Hb (SNO-Hb) plays a role in NO in the control of blood pressure and other NO-dependent reactions. We show th ... Full text Link to item Cite

Heme redox properties of S-nitrosated hemoglobin A0 and hemoglobin S: implications for interactions of nitric oxide with normal and sickle red blood cells.

Journal Article J Biol Chem · April 26, 2002 S-Nitrosated hemoglobin is remarkably stable and can be cycled between deoxy, oxygenated, or oxidized forms without significant loss of NO. Here we show that S-nitrosation of adult human hemoglobin (Hb A(0)) or sickle cell Hb (Hb S) results in an increased ... Full text Link to item Cite

Distinct domain responses of R-state human hemoglobins A, C, and S to anions.

Journal Article Blood cells, molecules & diseases · 2002 Anionic regulation of hemoglobin (Hb) is of increasing interest for the design of Hb-based oxygen carriers. Even "external" amino-acid substitutions can alter the nature and extent of anionic control. This was shown by evaluation of the anion sensitivities ... Cite

UV resonance raman study of β93-modified hemoglobin A: Chemical modifier-specific effects and added influences of attached poly(ethylene glycol) chains

Journal Article Biochemistry · 2002 The reactive sulfhydryl group on Cys β93 in human adult hemoglobin (HbA) has been the focus of many studies because of its importance both as a site for synthetic manipulation and as a possible binding site for nitric oxide (NO) in vivo. Despite the intere ... Full text Cite

β93 modified hemoglobin: Kinetic and conformational consequences

Journal Article Biochemistry · 2001 The reactive sulfhydryl on Cys β93 in human adult hemoglobin (HbA) has been the focus of much attention. It has purported functional roles such as a transporter of nitric oxide and a detoxifier of super oxide. In addition, it has a proposed role in the all ... Cite

Concentration-dependent effects of anions on the anaerobic oxidation of hemoglobin and myoglobin.

Journal Article The Journal of biological chemistry · December 2000 The redox potentials of hemoglobin and myoglobin and the shapes of their anaerobic oxidation curves are sensitive indicators of globin alterations surrounding the active site. This report documents concentration-dependent effects of anions on the ease of a ... Full text Cite

Effects of S-nitrosation on oxygen binding by normal and sickle cell hemoglobin.

Journal Article J Biol Chem · August 27, 1999 S-Nitrosated hemoglobin (SNO-Hb) is of interest because of the allosteric control of NO delivery from SNO-Hb made possible by the conformational differences between the R- and T-states of Hb. To better understand SNO-Hb, the oxygen binding properties of S- ... Full text Link to item Cite

Internal electron transfer between hemes and Cu(II) bound at cysteine beta93 promotes methemoglobin reduction by carbon monoxide.

Journal Article The Journal of biological chemistry · February 1999 Previous studies showed that CO/H2O oxidation provides electrons to drive the reduction of oxidized hemoglobin (metHb). We report here that Cu(II) addition accelerates the rate of metHb beta chain reduction by CO by a factor of about 1000. A mechanism wher ... Full text Cite

Spectroelectrochemistry of heme proteins: effects of active-site heterogeneity on Nernst plots.

Journal Article Bioelectrochemistry and bioenergetics (Lausanne, Switzerland) · February 1999 In order to detect and model the effect of functional chain heterogeneity on Nernst plots for heme proteins, we examined the redox properties of various myoglobins (Mbs) and their mixtures using an improved spectroelectrochemical method. Specific redox res ... Full text Cite

Disulfide bond reduction: A powerful, chemical probe for the study of structure-function relationships in the hemocyanins

Journal Article Archives of Biochemistry and Biophysics · 1999 The copper-containing hemocyanins are a class of oxygen-transport proteins whose structures differ in arthropods and molluscs. Crystal structure analyses and amino acid sequence comparisons show that disulfide bonding is a common feature in both arthropod ... Full text Cite

Conformational fluctuations in deoxy hemoglobin revealed as a major contributor to anionic modulation of function through studies of the oxygenation and oxidation of hemoglobins A0 and Deer Lodge beta2(NA2)His --> Arg.

Journal Article Biochemistry · January 1998 Organisms rely on regulation at the molecular level, such as the allosteric regulation of hemoglobin (Hb) function by anions, to meet challenges presented by changing environmental and physiological conditions. A comparison of the effects of anions on oxyg ... Full text Cite

Active-site disruption in native Limulus hemocyanin and its subunits by disulfide-bond reductants. A chemical probe for the study of structure- function relationships in the hemocyanins

Journal Article Archives of Biochemistry and Biophysics · 1998 The crystal structure analysis of Subunit II of Limulus hemocyanin has shown that its polypeptide chain is folded into three distinct structural domains. The oxygen-binding, dinuclear copper center is located deep in the core of Domain 2. Two disulfide bon ... Full text Cite

Stroma-free human hemoglobin A decreases R3230Ac rat mammary adenocarcinoma blood flow and oxygen partial pressure.

Journal Article Radiat Res · February 1997 We examined the effect of a nitric oxide (NO) quencher, stroma-free human hemoglobin A (HbA0; 0.01, 0.05, 0.1, 0.2 g/kg), on the blood flow measured using the Doppler flow technique, tumor oxygen pressure (pO2) and the diameter of the arterioles using R323 ... Link to item Cite

Healthy environments for healthy people: Bioremediation today and tomorrow

Journal Article Environmental Health Perspectives · 1997 Increases in environmental contamination lead to a progressive deterioration of environmental quality. This condition challenges our global society to find effective measures of remediation to reverse the negative conditions that severely threaten human an ... Cite

A carbon monoxide irreducible form of cytochrome c oxidase and other unusual properties of the "monomeric" shark enzyme.

Journal Article Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology · August 1996 Contrary to previous reports, the functional and spectral properties of "monomeric" shark cytochrome c oxidases are not entirely similar to those of the "dimeric" beef enzyme. Most significantly, unlike the behavior of beef oxidase, the fully oxidized shar ... Full text Cite

Structural basis for the root effect in haemoglobin.

Journal Article Nature structural biology · March 1996 The remarkable ability of root effect haemoglobins to pump oxygen against high O2 gradients results from extreme, acid-induced reductions in O2 affinity and cooperativity. The long-sought mechanism for the root effect, revealed by the 2 angstrom crystal st ... Full text Cite

S-nitrosohaemoglobin: a dynamic activity of blood involved in vascular control.

Journal Article Nature · March 1996 A dynamic cycle exists in which haemoglobin is S-nitrosylated in the lung when red blood cells are oxygenated, and the NO group is released during arterial-venous transit. The vasoactivity of S-nitrosohaemoglobin is promoted by the erythrocytic export of S ... Full text Cite

Keyhole limpet hemocyanin: structural and functional characterization of two different subunits and multimers.

Journal Article Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology · March 1996 Keyhole limpet hemocyanin (KLH), the large respiratory glycoprotein from the primitive gastropod mollusc, Megathura crenulata, is a potent immunogen used classically as a carrier protein for haptens and more recently in human vaccines and for immunotherapy ... Full text Cite

Nitrate binding to limulus polyphemus subunit type II hemocyanin and its functional implications

Journal Article Journal of Molecular Biology · 1996 The horseshoe crab, Limulus polyphemus, employs hemocyanin as an oxygen carrier in its hemolymph. This hemocyanin displays cooperative oxygen binding and heterotropic allosteric regulation by protons, chloride ions and divalent cations. Here, we report the ... Full text Cite

The site of the redox-linked proton pump in eukaryotic cytochrome c oxidases.

Journal Article FEBS letters · August 1995 The electronic spectra of fully oxidized derivatives of some cytochrome c oxidase preparations are distinctly pH dependent. In general, the observed spectral shifts are greater in the case of pulsed derivatives compared to resting preparations and also, gr ... Full text Cite

A spectroelectrochemical method for differentiation of steric and electronic effects in hemoglobins and myoglobins.

Journal Article The Journal of biological chemistry · June 1995 Spectroelectrochemical techniques are described which enable us to compare anion effects on redox curves of structurally distinct hemoglobins with oxygenation curves obtained under equivalent conditions. Nernst plots for tetrameric vertebrate Hbs show evid ... Full text Cite

Functional properties of the hemoglobin from the South American snake Mastigodryas bifossatus.

Journal Article Comparative biochemistry and physiology. Part A, Physiology · December 1994 The hemolysate of Mastigodryas bifossatus shows two major hemoglobins with very close isoelectric points, and four different globin chains. The stripped hemolysate exhibits a low alkaline Bohr effect (delta log P50/delta pH = -0.30 between pH 7 and 8) and ... Full text Cite

Acrylamide in polyacrylamide gels can modify proteins during electrophoresis.

Journal Article Anal Biochem · October 1994 Many notable discoveries have resulted from the characterization or purification of compounds by electrophoresis. The results reported here show that when polyacrylamide gels are used as the support matrix for electrophoresis, proteins can be modified by r ... Full text Link to item Cite

Crystallographic analysis of oxygenated and deoxygenated states of arthropod hemocyanin shows unusual differences.

Journal Article Proteins · August 1994 The X-ray structure of an oxygenated hemocyanin molecule, subunit II of Limulus polyphemus hemocyanin, was determined at 2.4 A resolution and refined to a crystallographic R-factor of 17.1%. The 73-kDa subunit crystallizes with the symmetry of the space gr ... Full text Cite

Chloride masks effects of opposing positive charges in Hb A and Hb Hinsdale (beta 139 Asn-->Lys) that can modulate cooperativity as well as oxygen affinity.

Journal Article Journal of molecular biology · June 1994 In the human hemoglobin variant Hb Hinsdale, lysine is substituted for asparagine at position beta 139 (H17), which lies in the water-filled cavity that runs through the center of the molecule. This substitution adds two extra cationic residues to the exce ... Full text Cite

A spectroelectrochemical method for evaluating factors which regulate the redox potential of hemoglobins

Journal Article Inorganica Chimica Acta · January 1, 1994 Spectroelectrochemical techniques were used to evaluate the redox potential of various hemoglobins under various experimental conditions. We use Ru(NH3)63+ as a redox mediator, which exchanges electrons with heme iron through an outer-sphere mechanism. Use ... Full text Cite

Nitric oxide binding to human ferrihemoglobins cross-linked between either alpha or beta subunits.

Journal Article Archives of biochemistry and biophysics · June 1993 We have examined the interactions between nitric oxide (NO) and oxidized human hemoglobin, comparing the behavior of unmodified HbA0 with that of two chemically modified hemoglobins. The latter are promising red cell substitute candidates due to their lowe ... Full text Cite

Crystal structure of deoxygenated Limulus polyphemus subunit II hemocyanin at 2.18 A resolution: clues for a mechanism for allosteric regulation.

Journal Article Protein science : a publication of the Protein Society · April 1993 The crystal structure of Limulus polyphemus subunit type II hemocyanin in the deoxygenated state has been determined to a resolution of 2.18 A. Phase information for this first structure of a cheliceratan hemocyanin was obtained by molecular replacement us ... Full text Cite

Consequences of chemical modifications on the free radical reactions of human hemoglobin.

Journal Article Archives of biochemistry and biophysics · October 1992 Hemoglobin-based oxygen carriers (HBOCs) are candidates for use as blood substitutes and resuscitation fluids. We determined that HBOCs of specific types differ in their ability to generate or interact with free radicals. The differences do not correlate w ... Full text Cite

Alteration of hemoglobin function by diadenosine 5',5'''-P1,P4- tetraphosphate and other alarmones

Journal Article Journal of Biological Chemistry · 1992 Heat-shocked organisms are known to produce not only 'heat shock proteins' but also diadenosine tetraphosphate (Ap4A) and related compounds that may act as 'alarmones' that alert the cell to the onset of metabolic stress. We found that Ap4A is synthesized ... Cite

Hemoglobin-based oxygen carriers (HBOCs): structural alterations that affect free radical generation.

Journal Article Biomaterials, artificial cells, and immobilization biotechnology : official journal of the International Society for Artificial Cells and Immobilization Biotechnology · January 1992 We examined how changes in oxygen affinity brought about by different chemical modifications of hemoglobins affect their oxidation-reduction reactions. The three modified hemoglobins studied were HbA-FMDA, HbBv-FMDA, produced by the reaction of human or bo ... Full text Cite

Hemoglobin-based oxygen carriers. Structural alterations that affect free radical formation

Journal Article Biomaterials, Artificial Cells, and Immobilization Biotechnology · December 1, 1991 Hemoglobin-based oxygen carriers (HBOCs) are candidates for use as blood substitutes and resuscitation fluids. We determined that the chemical modifications used to generate HBOCs of specific types alter their ability to generate or interact with free radi ... Cite

Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys beta 66----Thr) and its isolated beta chains.

Journal Article The Journal of biological chemistry · December 1991 Hemoglobin (Hb) Chico (Lys beta 66----Thr at E10) has a diminished oxygen affinity (Shih, D. T.-b., Jones, R. T., Shih, M. F.-C., Jones, M. B., Koler, R. D., and Howard, J. (1987) Hemoglobin 11, 453-464). Our studies show that its P50 is about twice that o ... Full text Cite

Oxidized dimeric Scapharca inaequivalvis. Co-driven perturbation of the redox equilibrium.

Journal Article The Journal of biological chemistry · September 1991 The dimeric hemoglobin isolated from Scapharca inaequivalvis, HbI, is notable for its highly cooperative oxygen binding and for the unusual proximity of its heme groups. We now report that the oxidized protein, an equilibrium mixture of a dimeric high spin ... Full text Cite

Interactions of nicotinamide adenine dinucleotides with varied states and forms of hemoglobin.

Journal Article The Journal of biological chemistry · July 1989 Spectrofluorometric techniques were used to quantify NADPH-hemoglobin interactions based on the quenching of NADPH fluorescence upon binding to hemoglobin. Fluorometric titrations were carried out with hemoglobin in varied states and with hemoglobins in wh ... Full text Cite

Isolation, purification and characterization of an iron-binding protein from the horseshoe crab (Limulus polyphemus).

Journal Article The Biochemical journal · May 1988 The presence of an iron-binding protein in the haemolymph of the horseshoe crab, Limulus polyphemus, was detected by gel filtration of 59Fe-labelled haemolymph. Lysis of amoebocytes did not change the amount of iron-binding protein in haemolymph samples. T ... Full text Cite

Allostery in Callinectes sapidus hemocyanin: cooperative oxygen binding and interactions with L-lactate, calcium, and protons.

Journal Article Biochemistry · March 1988 Allosteric interactions of Callinectes sapidus hemocyanin have been investigated by generation of precision oxygen-binding curves using a modified Imai apparatus and their subsequent analysis using numerical methods. The Monod-Wyman-Changeux (MWC) model, t ... Full text Cite

Active-site heterogeneity in Limulus hemocyanin as revealed by reaction with peroxides.

Journal Article Archives of biochemistry and biophysics · March 1988 Previously reported differences in the reactivities toward active-site ligands such as hydrogen peroxide indicate that the active-site geometries of the arthropod and mollusc hemocyanins are significantly different. Results are presented which demonstrate ... Full text Cite

Determination of L-lactate binding stoichiometry and differences in allosteric interactions of structurally distinct homohexamers from Panulirus interruptus hemocyanin.

Journal Article Biochimica et biophysica acta · December 1987 The role of structurally distinct subunits from the hemocyanin of Panulirus interruptus was investigated by the analysis of the oxygen-binding properties of reassembled homohexamers. Homohexamers reassembled from subunits a and b exhibited cooperative oxyg ... Full text Cite

Synthesis and characterization of iron(llI) chelating analogues of siderophores on organic solid supports

Journal Article Inorganica Chimica Acta · October 15, 1987 A series of iron(III)-selective chelating resins have been modeled after the structural features of the naturally occurring siderophore compounds with hydroxamate, catecholate and salicylate iron binding groups. Amberlite IRC-50 was derivatized via an acid ... Full text Cite

Fluorescence studies on the binding of reduced nicotinamide adenine dinucleotide phosphate to human hemoglobin A and its variant hemoglobin Providence.

Journal Article Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologicas · January 1987 The affinity constants for the binding of NADPH to human hemoglobin A were directly determined by fluorescence analysis since nucleotide fluorescence is quenched on binding to the protein. The binding constants 6.1 x 10(5), 5.02 x 10(5) and 1.2 x 10(5) wer ... Cite

The nicotinamide adenine dinucleotides as allosteric effectors of human hemoglobin.

Journal Article The Journal of biological chemistry · September 1986 The oxygen binding properties of human hemoglobin are appreciably altered by the nicotinamide dinucleotides NADH, NADP+, and NADPH. These cofactors are important in the control of many metabolic pathways and in providing reductive potential for a number of ... Full text Cite

Isolation of polypeptide chains with heme from the extracellular hemoglobin of Amphitrite ornata (Polychaeta, Annelida).

Journal Article Comparative biochemistry and physiology. B, Comparative biochemistry · January 1986 From the extracellular hemoglobin of Amphitrite ornata four constituent polypeptide chains containing heme and designated AI, AII, BI and BII according to the elution order were obtained by DE52-cellulose ion-exchange chromatography with dithiothreitol (DT ... Full text Cite

Kinetics of reduction of cytochrome c oxidase by dithionite and the effect of hydrogen peroxide.

Journal Article The Journal of biological chemistry · June 1985 The reduction of cytochrome c oxidase by dithionite was reinvestigated with a flow-flash technique and with varied enzyme preparations. Since cytochrome a3 may be defined as the heme in oxidase which can form a photolabile CO adduct in the reduced state, i ... Full text Cite

Structural and functional properties of hemoglobin from the vestimentiferan Pogonophora, Lamellibrachia

Journal Article Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular · May 20, 1985 Representatives of the phylum Pogonophora were found at 1800 m in a fault region off San Diego, CA, where there were indications of recently discharged hydrothermal fluids. The worm-like organisms were determined to be Lamellibrachia sp, phylogenetically r ... Full text Cite

Functional equivalence of monomeric (shark) and dimeric (bovine) cytochrome c oxidase.

Journal Article Journal of inorganic biochemistry · March 1985 Cytochrome c oxidase isolated from hammerhead shark red muscle is monomeric in relation to the dimeric form of isolated bovine cytochrome c oxidase but in other ways bears a close resemblance to the enzyme isolated from mammalian tissue [1, 2]. Comparative ... Full text Cite

Immunological correspondence between arthropod hemocyanin subunits. II. Xiphosuran (Limulus) and spider (Eurypelma, Cupiennius) hemocyanin.

Journal Article Biological chemistry Hoppe-Seyler · January 1985 The hemocyanins of the horseshoe crab Limulus polyphemus (48-mer), the tarantula Eurypelma californicum (24-mer), and the lycosid spider Cupiennius salei (dodecamer, hexamer) were dissociated into subunits, the subunits isolated and studied by two-dimensio ... Full text Cite

Carbon monoxide-driven reduction of ferric heme and heme proteins.

Journal Article The Journal of biological chemistry · September 1984 Oxidized cytochrome c oxidase in a carbon monoxide atmosphere slowly becomes reduced as shown by changes in its visible spectra and its reactivity toward oxygen. The "auto-reduction" of cytochrome c oxidase by this procedure has been used to prepare mixed ... Full text Cite

Self-association and oxygen-binding characteristics of the isolated subunits of Limulus polyphemus hemocyanin.

Journal Article Archives of biochemistry and biophysics · April 1984 The hemocyanin of the horseshoe crab Limulus polyphemus is characteristic of arthropod hemocyanins in that it is a high-molecular-weight oligomer composed of functionally and structurally distinct subunits. The protein forms a 48-subunit complex, the large ... Full text Cite

Paradoxical effects of methylmercury on the kinetics of cytochrome c oxidase.

Journal Article Biochemistry · February 1984 A stoichiometric amount of methylmercuric chloride substantially inhibits cytochrome c oxidase function under steady-state turnover conditions, where the enzyme is using its substrates, cytochrome c and oxygen, rapidly and continuously. Under these conditi ... Full text Cite

Underwater life support based on immobilized oxygen carriers.

Journal Article Applied biochemistry and biotechnology · February 1984 One of the primary problems that hinders humans in their efforts to explore and develop the ocean realms is the lack of a ready supply of oxygen. Practical methods have not yet been devised for using the vast amount of oxygen dissolved in ocean waters for ... Full text Cite

Allosteric modulation of Callinectes sapidus hemocyanin by binding of L-lactate.

Journal Article Biochemistry · February 1984 Hemocyanin of the blue crab Callinectes sapidus has the typical structure of crustacean hemocyanins in that its smallest in vivo structure is a hexamer of subunits each having a molecular mass of approximately 75 000. As found in the blood, Callinectes hem ... Full text Cite

Comparison of the physical and functional properties of the 48-subunit native molecule and the 24- and 12-subunit dissociation intermediates of Limulus polyphemus hemocyanin.

Journal Article Biochemistry · February 1984 Limulus hemocyanin is a 48-subunit complex that is composed of eight immunochemically distinct subunits.Conditions were established that allowed for comparison of the structural and functional properties of the native molecule with those of its 24-subunit ... Full text Cite

Metal ion interactions with Limulus polyphemus and Callinectes sapidus hemocyanins: stoichiometry and structural and functional consequences of calcium(II), cadmium(II), zinc(II), and mercury(II) binding.

Journal Article Biochemistry · September 1983 Hemocyanins are oligomeric metalloproteins containing binuclear copper centers that reversibly combine with oxygen molecules. The structural stability and functional properties of these proteins are modified by divalent cations. Equilibrium dialysis was us ... Full text Cite

Assembly and calcium-induced cooperativity of Limulus IV hemocyanin: a model system for analysis of structure-function relationships in the absence of subunit heterogeneity.

Journal Article Biochemistry · September 1983 Hemocyanins, the high molecular weight copper proteins which serve as oxygen carriers in many arthropods and molluscs, are representative of multisubunit complexes which are capable of reversible dissociation and assembly. Although reversible, in many hemo ... Full text Cite

Haemocyanins

Journal Article Journal of Chromatography Library · January 1, 1983 This chapter discusses electrophoretic techniques that have played a significant role in detecting and studying subunit heterogeneity. Charge heterogeneity is not readily detectable by other techniques. It plays a major role in the subsequent purification ... Full text Cite

Cytochrome c oxidase binding of hydrogen peroxide.

Journal Article Biochemistry · May 1982 Oxidized cytochrome c oxidase can bind hydrogen peroxide, as evidenced by changes in its spectrum and its ability to use hydrogen peroxide as an electron acceptor in cytochrome c oxidation. The affinity of the oxidized enzyme for hydrogen peroxide is high, ... Full text Cite

Heavy metal ion interactions with Callinectes sapidus hemocyanin: structural and functional changes induced by a variety of heavy metal ions.

Journal Article Biochemistry · May 1982 Hemocyanins are oligomeric proteins that reversibly bind oxygen. The oxygen binding site is a binuclear copper center bound to the protein by amino acid side chains. The hemocyanin of the blue crab, Callinectes sapidus, occurs in vivo as a mixture of 25S d ... Full text Cite

Chloride and pH dependence of cooperative interactions in Limulus polyphemus hemocyanin.

Journal Article Progress in clinical and biological research · January 1982 Cite

Hemocyanin of the chambered nautilus: structure-function relationships.

Journal Article Archives of biochemistry and biophysics · October 1981 Full text Cite

Subunit composition of high molecular weight oligomer: Limulus polyphemus hemocyanin.

Journal Article Archives of biochemistry and biophysics · September 1981 Full text Cite

Amphitrite ornata erythrocruorin. II. Molecular controls of function.

Journal Article Biochimica et biophysica acta · August 1981 In the marine terebellid worm Amphitrite ornata the vascular fluid contains a high molecular weight erythrocruorin, while cells of the coelom contain a monomeric hemoglobin. The structural integrity of the erythrocruorin molecule is known to be dependent o ... Full text Cite

Preparation of high molecular weight invertebrate hemoglobins.

Journal Article Methods in enzymology · January 1981 Full text Cite

Anionic control of function in vertebrate hemoglobins

Journal Article Integrative and Comparative Biology · December 1, 1980 Point mutations in the amino acid sequence of normal human hemoglobin have provided a powerful means of probing structure-function relationships in this respiratory protein. Through studies of specific hemoglobin variants it has been possible to gain a bet ... Full text Cite

Hemocyanins relationships in their structure, function and assembly

Journal Article Integrative and Comparative Biology · December 1, 1980 Hemocyanins are high molecular weight oxygen-carrying proteins that occur in the molluscs and arthropods. The oxygen-binding site in these proteins is a pair of copper atoms bound directly to ammo acid side chains. The biscopper sites of these proteins bin ... Full text Cite

Amphitrite ornata erythrocruorin. I. Structural properties and characterization of subunit interactions.

Journal Article Biochimica et biophysica acta · May 1980 A high molecular weight erythrocruorin (Mr approx. 3 . 10(6)) is found in the vascular system of the marine terebellid worm Amphitrite ornata, while a low molecular weight hemoglobin is contained in the coelomic cells. Polyacrylamide gel electrophoresis in ... Full text Cite

Structural and functional properties of cytochrome c oxidases isolated from sharks.

Journal Article The Journal of biological chemistry · April 1980 Full text Cite

Competition in oxygen-linked anion binding to normal and variant human hemoglobins.

Journal Article Hemoglobin · January 1980 The two-state model of Monod, Wyman and Changeux has been used extensively in analysis of the functional behavior of human hemoglobin. Within the context of this model, the cooperativity, pH dependence of oxygen binding, and anionic regulation of oxygen af ... Full text Cite

Kinetics of oxygen and carbon monoxide binding to the hemoglobins of the water snakes Liophis miliaris and Helicops modestus

Journal Article Comparative Biochemistry and Physiology -- Part B: Biochemistry and · January 1, 1980 1. 1. Liophis miliaris and Helicops modestus are water snakes having different respiratory adaptiations to their specific habitats. L. miliaris is more active and spends more time on land than H. modestus. Knowledge of the equilibrium and kinetics of ligan ... Full text Cite

Oxygen equilibria and ligand-binding kinetics of erythrocruorins from two burrowing polychaetes of different modes of life, Marphysa sanguinea and Diopatra cuprea

Journal Article Journal of Comparative Physiology □ B · June 1, 1978 Oxygen equilibria, ligand-binding kinetics and some other physicochemical properties are reported for erythrocruorins of two intertidal polychaetes:Marphysa sanguinea, which inhabits simple, relatively stagnant burrows, and Diopatra cuprea, which inhabits ... Full text Cite

Functional properties of Aplysia brasiliana myoglobin

Journal Article Comparative Biochemistry and Physiology · 1978 Cite

Purification and thermal denaturation of aplysia Brasiliana myoglobin

Journal Article IRCS Medical Science: Biochemistry · January 1, 1978 Cite

Functional properties of normal and sickle cell hemoglobins in polyethylene glycol 6000.

Journal Article Biochimica et biophysica acta · December 1977 The functional properties of human hemoglobin A and S were studied in concentrated solutions of polyethylene glycol. Polyethylene glycol solutions are frequently used as media for protein crystallization. In particular, sickle cell hemoglobin, which does n ... Full text Cite

Oxygen binding domains of Helisoma trivolvis hemoglobin.

Journal Article Biochimica et biophysica acta · October 1977 Full text Cite

Hemoglobins of two terebellid polychaetes: Enoplobranchus sanguineus and Amphitrite ornata.

Journal Article Comparative biochemistry and physiology. A, Comparative physiology · January 1977 Full text Cite

Hemocyanin of the horseshoe crab, Limulus polyphemus. Structural differentiation of the isolated components.

Journal Article The Journal of biological chemistry · December 1976 The high molecular weight hemocyanin found in the hemolymph of the horseshoe crab, Limulus polyphemus, is composed of at least eight different kinds of subunits. Ion exchange chromatography at high pH in the presence of EDTA yields five major zones, hemocy ... Full text Cite

Hemoglobin providence. Functional consequences of two alterations of the 2,3-diphosphoglycerate binding site at position beta 82.

Journal Article The Journal of biological chemistry · December 1976 Position beta 82 in human hemoglobin (Hb) is normally occupied by lysine, a positively charged residue that is involved in the binding of anionic cofactors. This residue is substituted by a neutral residue in Hb Providence Asn and by a negatively charged r ... Full text Cite

Functional consequences of ligand-linked dissociation in hemoglobin from the sea cucumber Molpadia arenicola.

Journal Article Biochimica et biophysica acta · May 1976 It has been established that Molpadia hemoglobin tends to dissociate into subunits as oxygen is bound. The kinetics and equilibria of carbon monoxide and ethylisocyanide binding reported here show a dependence on protein concentration that supports the con ... Full text Cite

The hemoglobin system of the primitive fish, Amia calva: isolation and functional characterization of the individual hemoglobin components.

Journal Article Biochimica et biophysica acta · May 1976 Blood from the primitive holostean fish, the bowfin, Amia calva, contains 2 mo of ATP per mol of hemoglobin. The hemolysates contain at least five tetrameric hemoglobin components which differ in their oxygen affinities and their response to cofactors such ... Full text Cite

Spot hemoglobin. Studies on the Root effect hemoglobin of a marine teleost.

Journal Article The Journal of biological chemistry · April 1976 The Spot, Leiostomus xanthrus, has a single tetrameric hemoglobin. Structural studies indicate the presence of alpha- and beta-like chains with COOH-terminal sequences of --Arg and --TYR-His, respectively, the same as is found in human hemoglobin. Spot hem ... Full text Cite

Hemoglobins of Boa constrictor amarali

Journal Article Comparative Biochemistry and Physiology · 1976 Cite

Hemoglobin Deer Lodge (beta 2 His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site.

Journal Article The Journal of biological chemistry · December 1975 Hemoglobin Deer Lodge is an abnormal human hemoglobin with arginine substituted for histidine at the beta 2 position. X-ray crystallography of normal human hemoglobin has shown that the beta 2 residue is normally part of the binding site for 2,3-diphosphog ... Full text Cite

Hemoglobins and hemocyanins: comparative aspects of structure and function.

Journal Article The Journal of experimental zoology · October 1975 Comparative studies of protein structure and function can be quite interesting by themselves, and even more interesting when interpreted with respect to an animal's physiology. In the case of fish hemoglobins, some success in the latter has been achieved b ... Full text Cite

Allosteric interactions in non-alpha chains isolated from normal human hemoglobin, fetal hemoglobin, and hemoglobin Abruzzo (beta143 (H21) His replaced by Arg).

Journal Article The Journal of biological chemistry · August 1975 Oxygen-linked effects of inositol hexaphosphate occur in heme-containing non-alpha chains isolated from normal human hemoglobin, fetal hemoglobin, and the abnormal human hemoglobin Abruzzo, beta143(H21) His leads to Arg. The occurrence of these effects imp ... Full text Cite

Hemoglobin Abruzzo (beta143 (H21) His replaced by Arg). Consequences of altering the 2,3-diphosphoglycerate binding site.

Journal Article The Journal of biological chemistry · August 1975 Hemoglobin Abruzzo is an abnormal human hemoglobin with a substitution at a residue known to be involved in the binding of 2,3-diphosphoglyceric acid. It has increased oxygen affinity and reduced heme-heme interaction in the absence of organic or inorganic ... Full text Cite

The structure and evolution of parvalbumins. I. Amino acid compositional studies of parvalbumins from four perciform species.

Journal Article Journal of molecular evolution · July 1975 1. Parvalbumins were isolated from the white muscle of Cynoscion regalis, Leiostomus xanthurus, and Menticirrhus americanus of the Sciaenidae and Pomatomus saltatrix of the Pomatomidae. 2. Menticirrhus contains three isoparvalbumins. The other species cont ... Full text Cite

The role of coelomic and vascular hemoglobin in the annelid family Terebellidae

Journal Article Comparative Biochemistry and Physiology · 1975 Cite

Urea tolerance as a molecular adaptation of elasmobranch hemoglobins.

Journal Article Science (New York, N.Y.) · October 1974 Urea is maintained at moderately high concentrations in the blood and tissues of marine elasmobranchs. Functional properties of the hemoglobins fromn several elasmobranch species are unaffected by urea concentrations as high as 5 molar. This in. sensitivit ... Full text Cite

Functional differences in the multiple hemocyanins of the horseshoe crab, Limulus polyphemus L.

Journal Article Proceedings of the National Academy of Sciences of the United States of America · June 1974 Hemocyanin in the hemolymph of the horseshoe crab, Limulus polyphemus L., is a high-molecular-weight copper protein which binds oxygen cooperatively and shows a higher oxygen affinity at pH 7 than at pH 9. Treatment with EDTA (ethylenediaminetetra-acetate) ... Full text Cite

Effect of pH and anions on functional properties of hemoglobin from Lemur fulvus fulvus.

Journal Article The Journal of biological chemistry · June 1974 Full text Cite

Functional properties of carboxypeptidase-digested hemoglobins.

Journal Article Journal of molecular biology · February 1974 Full text Cite

Functional properties of hemoglobin Leiden (α2(A)β2(6 or 7 Glu deleted))

Journal Article Archives of Biochemistry and Biophysics · 1974 Hemoglobin Leiden is an abnormal human hemoglobin in which a glutamic acid residue was deleted from the β chain at position 6 or 7. The α amino groups of the β chain N termini in tetrameric hemoglobin A are thought to be directly involved in the binding of ... Cite

Hemoglobins from trout: structural and functional properties.

Journal Article Molecular and cellular biochemistry · June 1973 Full text Cite

Effect of steady illumination on the binding of carbon monoxide by carboxymethylated cytochrome c.

Journal Article The Biochemical journal · April 1973 The quantum yield, [unk], is reported for the photodissociation of CO from reduced carboxymethylated cytochrome c. The values of [unk] obtained are low relative to that for myoglobin and are pH-independent, being 0.23 at pH6.1 and 0.27 at pH9.7. ... Full text Cite

Partial restoration of normal functional properties in carboxypeptidase A-digested hemoglobin.

Journal Article Proceedings of the National Academy of Sciences of the United States of America · August 1972 In the absence of organic phosphates human hemoglobin A digested with carboxypeptidase A (des His, Tyr beta) has high ligand affinity, a greatly reduced Bohr effect, and no heme-heme interaction. Under these conditions, it shows the simple, homogeneous lig ... Full text Cite

Carbon monoxide binding by hemoglobin and myoglobin under photodissociating conditions.

Journal Article Proceedings of the National Academy of Sciences of the United States of America · April 1972 Carbon monoxide binding by myoglobin and hemoglobin has been studied under conditions of constant illumination. For hemoglobin, the homotropic heme-heme interaction (cooperativity) and the heterotropic Bohr effect are invariant with light intensity over a ... Full text Cite

Kinetic and spectral resolution of two components of delayed emission from Chlorella pyrenoidosa

Journal Article BBA - Bioenergetics · 1971 1. Decay kinetics of delayed emission from Chlorella pyrenoidosa have been determined with a high degree of precision. The decay in the msec-to-sec interval after excitation can be represented accurately by the sum of two exponential decays-a "fast compone ... Cite

Fluorescence and oxygen evolution from Chlorella pyrenoidosa

Journal Article BBA - Bioenergetics · 1969 The process of photosynthetic energy conversion in Chlorella pyrenoidosa was investigated by simultaneous measurement of transient and steady-state rates of O 2 evolution and fluorescence. 1. 1. Alternation or superimposition of lig ... Cite