Rational design of nascent metalloenzymes.

@article{citeulike:2723990, abstract = {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.}, address = {Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.}, author = {Benson, D. E. and Wisz, M. S. and Hellinga, H. W. }, citeulike-article-id = {2723990}, issn = {0027-8424}, journal = {Proceedings of the National Academy of Sciences of the United States of America}, keywords = {protein\_design}, month = {June}, number = {12}, pages = {6292--6297}, posted-at = {2008-04-27 15:25:48}, priority = {2}, title = {Rational design of nascent metalloenzymes.}, url = {http://view.ncbi.nlm.nih.gov/pubmed/10841535}, volume = {97}, year = {2000} }

TY - JOUR ID - citeulike:2723990 L3 - citeulike-article-id:2723990 TI - Rational design of nascent metalloenzymes. JF - Proceedings of the National Academy of Sciences of the United States of America VL - 97 IS - 12 SP - 6292 EP - 6297 AD - Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA. SN - 0027-8424 N2 - 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. KW - protein_design AU - Benson, DE AU - Wisz, MS AU - Hellinga, HW PY - 2000/06/06/ UR - http://view.ncbi.nlm.nih.gov/pubmed/10841535 ER -