A Cysteine-Rich CCG Domain Contains a Novel [4Fe-4S] Cluster Binding Motif As Deduced from Studies with Subunit B of Heterodisulfide Reductase from Methanothermobacter marburgensis-Reference-Cited by-同舟云学术

A Cysteine-Rich CCG Domain Contains a Novel [4Fe-4S] Cluster Binding Motif As Deduced from Studies with Subunit B of Heterodisulfide Reductase from Methanothermobacter marburgensis

Published:2007-10-12 Issue:44 Volume:46 Page:12875-12885
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Hamann Nils¹,Mander Gerd J.¹,Shokes Jacob E.¹,Scott Robert A.¹,Bennati Marina¹,Hedderich Reiner¹

Affiliation:

1. Max Planck Institute for Terrestrial Microbiology, Karl-von-Frisch Strasse, D-35043 Marburg, Germany, Department of Chemistry and Center for Metalloenzyme Studies, University of Georgia, Athens, Georgia 30602-2556, and Institute of Physical and Theoretical Chemistry and Center for Biomolecular Magnetic Resonance, J. Goethe University of Frankfurt, D-60438 Frankfurt, Germany

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi700679u

Reference43 articles.

1. Anaerobic respiration with elemental sulfur and with disulfides

2. Purification and properties of heterodisulfide reductase from Methanobacterium thermoautotrophicum (strain Marburg)

3. Heterodisulfide Reductase from Methanol-Grown Cells of Methanosarcina Barkeri is not a Flavoenzyme

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