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Licensed Unlicensed Requires Authentication Published by De Gruyter 2020

11. Nickel, Iron, Sulfur Sites

From the book Transition Metals and Sulfur – A Strong Relationship for Life

  • Yulia Ilina , Berta M. Martins , Jae-Hun Jeoung and Holger Dobbek

Abstract

Enzymes relying on the interplay of nickel, iron, and sulfur in their active sites are used by prokaryotes to catalyze reactions driving the global carbon and hydrogen cycles. The three enzymes, [NiFe] hydrogenases, Ni,Fe-containing carbon monoxide dehydrogenases and acetyl-CoA synthases share an ancient origin possibly derived from abiotic processes. Although their active sites have different compositions and assemble Ni, Fe, and S in different ways and for different purposes, they share a central role of Ni in substrate binding and activation, with sulfur linking the Ni ion to one or more Fe ions, which, although indispensable for function, supports the catalytic process in less understood ways. The review gives a short overview on the properties of the three individual enzymes highlighting their parallels and differences.

© 2020 Walter de Gruyter GmbH, Berlin/Munich/Boston
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