Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 6 August 1993:
Vol. 261. no. 5122, pp. 701 - 708
DOI: 10.1126/science.7688141
Prev | Table of Contents | Next

Articles

Science, Vol 261, Issue 5122, 701-708
Copyright © 1993 by American Association for the Advancement of Science

articles

Metalloenzymes, structural motifs, and inorganic models

KD Karlin

Department of Chemistry, Johns Hopkins University, Baltimore, MD 21218.

Metalloenzymes effect a variety of important chemical transformations, often involving small molecule substrates or products such as molecular oxygen, hydrogen, nitrogen, and water. A diverse array of ions or metal clusters is observed at the active-site cores, but living systems use basic recurring structures that have been modified or tuned for specific purposes. Inorganic chemists are actively involved in the elucidation of the structure, spectroscopy, and mechanism of action of these biological catalysts, in part through a synthetic modeling approach involving biomimetic studies.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Involvement of a novel copper chaperone in tyrosinase activity and melanin synthesis in Marinomonas mediterranea.
D. Lopez-Serrano, F. Solano, and A. Sanchez-Amat (2007)
Microbiology 153, 2241-2249
   Abstract »    Full Text »    PDF »
Dioxygen Binds End-On to Mononuclear Copper in a Precatalytic Enzyme Complex.
S. T. Prigge, B. A. Eipper, R. E. Mains, and L. M. Amzel (2004)
Science 304, 864-867
   Abstract »    Full Text »    PDF »
Iron Requirement for GAL Gene Induction in the Yeast Saccharomyces cerevisiae.
X. Shi, K. Chabarek, A. Budai, and Z. Zhu (2003)
J. Biol. Chem. 278, 43110-43113
   Abstract »    Full Text »    PDF »
Specific Potassium Binding Stabilizes pI258 Arsenate Reductase from Staphylococcus aureus.
N. Lah, J. Lah, I. Zegers, L. Wyns, and J. Messens (2003)
J. Biol. Chem. 278, 24673-24679
   Abstract »    Full Text »    PDF »
Ferric Ions Are Essential for the Biological Activity of the Hormone Glycine-extended Gastrin.
J. Pannequin, K. J. Barnham, F. Hollande, A. Shulkes, R. S. Norton, and G. S. Baldwin (2002)
J. Biol. Chem. 277, 48602-48609
   Abstract »    Full Text »    PDF »
A Copper-responsive Transcription Factor, CRF1, Mediates Copper and Cadmium Resistance in Yarrowia lipolytica.
S. Garcia, M. Prado, R. Degano, and A. Dominguez (2002)
J. Biol. Chem. 277, 37359-37368
   Abstract »    Full Text »    PDF »
Distinct roles for two N-terminal cleaved domains in mitochondrial import of the yeast frataxin homolog, Yfh1p.
D. M. Gordon, M. Kogan, S. A.B. Knight, A. Dancis, and D. Pain (2001)
Hum. Mol. Genet. 10, 259-269
   Abstract »    Full Text »    PDF »
Reactive oxygen species in cell signaling.
V. J. Thannickal and B. L. Fanburg (2000)
Am J Physiol Lung Cell Mol Physiol 279, L1005-L1028
   Abstract »    Full Text »    PDF »
Copper Differentially Regulates the Activity and Degradation of Yeast Mac1 Transcription Factor.
Z. Zhu, S. Labbe, Ma. M. O. Pena, and D. J. Thiele (1998)
J. Biol. Chem. 273, 1277-1280
   Abstract »    Full Text »    PDF »
Amidation of Bioactive Peptides: The Structure of Peptidylglycine alpha -Hydroxylating Monooxygenase.
S. T. Prigge, A. S. Kolhekar, B. A. Eipper, R. E. Mains, and L. M. Amzel (1997)
Science 278, 1300-1305
   Abstract »    Full Text »
Bioinorganic chemistry: a maturing frontier.
S. Lippard (1993)
Science 261, 699-700
   PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)