Great metalloclusters in enzymology
Metallocluster-containing enzymes catalyze some of the most basic redox transformations in the biosphere. The reactions catalyzed by these enzymes typically involve small molecules such as N2, CO, and H2 that are used to generate both chemical building blocks and energy for metabolic purposes. During the past decade, structures have been established for the iron-sulfur-based metalloclusters present in the molybdenum nitrogenase, the iron-only hydrogenase, and the nickel-carbon monoxide dehydrogenase, and for the copper-sulfide-based cluster in nitrous oxide reductase. Although these clusters are built from interactions observed in simpler metalloproteins, they contain novel features that may be relevant for their catalytic function. The mechanisms of metallocluster-containing enzymes are still poorly defined, and represent substantial and continuing challenges to biochemists, biophysicists, and synthetic chemists. These proteins also provide a window into the union of the biological and inorganic worlds that may have been relevant to the early evolution of biochemical catalysis.
"Reprinted, with permission, from the Annual Review of Biochemistry, Volume 71 copyright 2002 by Annual Reviews, www.annualreviews.org" Discussions with James B. Howard, Benedikt Schmid, Jessica Chiu, Pavel Strop, Oliver Einsle, and Akif Tezcan are, as always, greatly appreciated. Research in the author's laboratory was supported in part by U.S. Public Health Service grant GM45162.
Published - REEarb02.pdf