Structural basis of the redox switches in the NAD + -reducing soluble [NiFe]-hydrogenase-Reference-Cited by-同舟云学术

Structural basis of the redox switches in the NAD + -reducing soluble [NiFe]-hydrogenase

Published:2017-09 Issue:6354 Volume:357 Page:928-932
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Shomura Y.¹^ORCID,Taketa M.²³^ORCID,Nakashima H.²,Tai H.³⁴^ORCID,Nakagawa H.²,Ikeda Y.²^ORCID,Ishii M.⁵,Igarashi Y.⁵,Nishihara H.⁶,Yoon K.-S.⁷⁸^ORCID,Ogo S.⁷⁸^ORCID,Hirota S.³⁴^ORCID,Higuchi Y.²³⁸^ORCID

Affiliation:

1. Institute of Quantum Beam Science, Graduate School of Science and Engineering, Ibaraki University, 4-12-1 Nakanarusawa, Hitachi, Ibaraki 316-8511, Japan.

2. Department of Picobiology, Graduate School of Life Science, University of Hyogo, 3-2-1 Koto, Kamigori-cho, Ako-gun, Hyogo 678-1297, Japan.

3. Core Research for Evolutional Science and Technology (CREST), Japan and Science Technology Agency, 4-1-8 Honcho, Kawaguchi, Saitama 332-0012, Japan.

4. Graduate School of Materials Science, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma, Nara 630-0192, Japan.

5. Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-8657, Japan.

6. Department of Bioresource Science, College of Agriculture, Ibaraki University, 3-21-1, Chu-ou, Ami, Ibaraki 300-0393, Japan.

7. World Premier International Research Center Initiative–International Institute for Carbon Neutral Energy Research (WPI-I2CNER), Kyushu University, 744 Moto-oka, Nishi-ku, Fukuoka 819-0395, Japan.

8. SPring-8 Center, RIKEN, 1-1-1 Koto, Sayo-cho, Sayo-gun, Hyogo 679-5148, Japan.

Abstract

How a hydrogenase protects its active site Hydrogen-metabolizing organisms use an [NiFe]-hydrogenase to catalyze hydrogen oxidation. One type of [NiFe]-hydrogenase, the NAD + -reducing soluble [NiFe]-hydrogenase (SH), couples reduction of NAD + to the oxidation of hydrogen. Shomura et al. solved the structure of SH from an H 2 -oxidizing bacterium in both the air-oxidized and the active reduced state. In the reduced state, the NiFe catalytic center in SH has the same ligand coordination as in other [NiFe]-hydrogenases. However, the air-oxidized active site has an unusual coordination geometry that would prevent O 2 from accessing the site and so may protect against irreversible oxidation. Science , this issue p. 928

Funder

ENEOS Hydrogen Trust Fund

JSPS

Challenging Exploratory Research

JST CREST

The Mitsubishi Foundation

Scientific Research on Innovative Areas

Young Scientists B

JSPS Grants-in-Aid Specially Promoted Research

Publisher

American Association for the Advancement of Science (AAAS)

Subject