A site-differentiated [4Fe–4S] cluster controls electron transfer reactivity of <i>Clostridium acetobutylicum</i> [FeFe]-hydrogenase I-Reference-Cited by-同舟云学术

A site-differentiated [4Fe–4S] cluster controls electron transfer reactivity of Clostridium acetobutylicum [FeFe]-hydrogenase I

Published:2022 Issue:16 Volume:13 Page:4581-4588
ISSN:2041-6520
Container-title:Chemical Science
language:en
Short-container-title:Chem. Sci.

Author:

Lubner Carolyn E.¹^ORCID,Artz Jacob H.¹,Mulder David W.¹^ORCID,Oza Aisha¹,Ward Rachel J.²,Williams S. Garrett³⁴,Jones Anne K.³^ORCID,Peters John W.⁵^ORCID,Smalyukh Ivan I.²⁶^ORCID,Bharadwaj Vivek S.¹^ORCID,King Paul W.¹⁶^ORCID

Affiliation:

1. National Renewable Energy Laboratory, Golden, Colorado, USA

2. Department of Physics, University of Colorado Boulder, Boulder, Colorado, USA

3. School of Molecular Sciences, Arizona State University, Tempe, Arizona, USA

4. Sandia National Laboratories, Albuquerque, New Mexico, USA

5. Institute of Biological Chemistry, Washington State University, Pullman, Washington, USA

6. Renewable and Sustainable Energy Institute, National Renewable Energy Laboratory and University of Colorado Boulder, Boulder, Colorado, USA

Abstract

Histidine coordination of the distal [4Fe–4S] cluster in [FeFe]-hydrogenase was demonstrated to tune the cluster spin-states, spin-pairing and surrounding molecular orbitals to enable more facile electron transfer compared to cysteine coordination.

Funder

National Institutes of Health

U.S. Department of Agriculture

National Institute of Food and Agriculture

US Department of Energy's Basic Energy Sciences

Publisher

Royal Society of Chemistry (RSC)

Subject

General Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2022/SC/D1SC07120C

Reference48 articles.