Rational design of nascent metalloenzymes.

Published

Journal Article

Understanding the early genesis of new enzymatic functions is one of the challenges in protein design, mechanistic enzymology, and molecular evolution. We have experimentally mimicked starting points in this process by introducing primitive iron and oxygen binding sites at various locations in thioredoxin, a small protein lacking metal centers, by using computational design. These rudimentary active sites show emerging enzymatic activities that select to varying degrees between different oxygen chemistries. Even within these nascent enzymes, mechanisms by which different reactions are controlled can be discerned. These involve both stabilizing and destabilizing interactions imposed on the metal center by the surrounding protein matrix.

Full Text

Duke Authors

Cited Authors

  • Benson, DE; Wisz, MS; Hellinga, HW

Published Date

  • June 6, 2000

Published In

Volume / Issue

  • 97 / 12

Start / End Page

  • 6292 - 6297

PubMed ID

  • 10841535

Pubmed Central ID

  • 10841535

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.97.12.6292

Language

  • eng

Conference Location

  • United States