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

Publication ,  Journal Article
Bonaventura, C; Henkens, R; De Jesus-Bonilla, W; Lopez-Garriga, J; Jia, Y; Alayash, AI; Siburt, CJP; Crumbliss, AL
Published in: 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 were found to be more rapidly oxidized by nitrite than any previously studied Hb, while those of Lucina Hb II showed an unprecedented resistance to oxidation induced by nitrite. Nitrite-induced oxidation of Lucina Hb II was enabled only when O₂ was removed from its active site. Structural analysis revealed that O₂ "clams up" the active site by hydrogen bond formation to B10Tyr and other distal-side residues. Quaternary effects further restrict nitrite entry into the active site and stabilize the hydrogen-bonding network in oxygenated Lucina Hb II dimers. The dramatic differences in nitrite reactivities of the Lucina Hbs are not related to their O₂ affinities or anaerobic redox potentials, which were found to be similar, but are instead a result of differences in accessibility of nitrite to their active sites; i.e. these differences are due to a kinetic rather than thermodynamic effect. Comparative studies revealed heme accessibility to be a factor in human Hb oxidation by nitrite as well, as evidenced by variations of rates of nitrite-induced oxidation that do not correlate with R and T state differences and inhibition of oxidation rate in the presence of O₂. These results provide a dramatic illustration of how evolution of active sites with varied heme accessibility can moderate the rates of inner-sphere oxidative reactions of Hb and other heme proteins.

Duke Scholars

Published In

Biochimica et biophysica acta

DOI

EISSN

1878-2434

ISSN

0006-3002

Publication Date

October 2010

Volume

1804

Issue

10

Start / End Page

1988 / 1995

Related Subject Headings

  • Oxygen
  • Oxidation-Reduction
  • Nitrites
  • Kinetics
  • Hydrogen Bonding
  • Humans
  • Hemoglobins
  • Heme
  • Bivalvia
  • Binding Sites
 

Citation

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MLA
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Bonaventura, C., Henkens, R., De Jesus-Bonilla, W., Lopez-Garriga, J., Jia, Y., Alayash, A. I., … Crumbliss, A. L. (2010). Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite. Biochimica et Biophysica Acta, 1804(10), 1988–1995. https://doi.org/10.1016/j.bbapap.2010.06.016
Bonaventura, Celia, Robert Henkens, Walleska De Jesus-Bonilla, Juan Lopez-Garriga, Yiping Jia, Abdu I. Alayash, Claire J Parker Siburt, and Alvin L. Crumbliss. “Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite.Biochimica et Biophysica Acta 1804, no. 10 (October 2010): 1988–95. https://doi.org/10.1016/j.bbapap.2010.06.016.
Bonaventura C, Henkens R, De Jesus-Bonilla W, Lopez-Garriga J, Jia Y, Alayash AI, et al. Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite. Biochimica et biophysica acta. 2010 Oct;1804(10):1988–95.
Bonaventura, Celia, et al. “Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite.Biochimica et Biophysica Acta, vol. 1804, no. 10, Oct. 2010, pp. 1988–95. Epmc, doi:10.1016/j.bbapap.2010.06.016.
Bonaventura C, Henkens R, De Jesus-Bonilla W, Lopez-Garriga J, Jia Y, Alayash AI, Siburt CJP, Crumbliss AL. Extreme differences between hemoglobins I and II of the clam Lucina pectinalis in their reactions with nitrite. Biochimica et biophysica acta. 2010 Oct;1804(10):1988–1995.

Published In

Biochimica et biophysica acta

DOI

EISSN

1878-2434

ISSN

0006-3002

Publication Date

October 2010

Volume

1804

Issue

10

Start / End Page

1988 / 1995

Related Subject Headings

  • Oxygen
  • Oxidation-Reduction
  • Nitrites
  • Kinetics
  • Hydrogen Bonding
  • Humans
  • Hemoglobins
  • Heme
  • Bivalvia
  • Binding Sites