Jump to ContentJump to Main Navigation
Show Summary Details
More options …

Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred

12 Issues per year


IMPACT FACTOR 2016: 3.273

CiteScore 2016: 3.01

SCImago Journal Rank (SJR) 2016: 1.679
Source Normalized Impact per Paper (SNIP) 2016: 0.800

Online
ISSN
1437-4315
See all formats and pricing
More options …
Volume 381, Issue 9-10 (Sep 2000)

Issues

The Role of Se, Mo and Fe in the Structure and Function of Carbon Monoxide Dehydrogenase

Ortwin Meyer / Lothar Gremer / Reinhold Ferner / Marion Ferner / Holger Dobbek / Manuel Gnida / Wolfram Meyer-Klaucke / Robert Huber
Published Online: 2005-07-05 | DOI: https://doi.org/10.1515/BC.2000.108

Abstract

CO dehydrogenase (EC 1.2.99.2) catalyzes the oxidation of CO according to the following equation: CO + H2O → CO2 + 2 e + 2 H+. It is a selenium-containing molybdo-iron-sulfur-flavoenzyme, which has been crystallized and structurally characterized in its oxidized state from the aerobic CO utilizing bacteria Oligotropha carboxidovorans and Hydrogenophaga pseudoflava. Both CO dehydrogenase structures show only minor differences, and the enzymes are dimers of two heterotrimers. Each heterotrimer is composed of a molybdoprotein, a flavoprotein, and an iron-sulfur protein. CO oxidation takes place at the molybdoprotein which contains a 1:1 mononuclear complex of molybdopterin-cytosine dinucleotide and a Mo-ion, along with a catalytically essential S-selanylcysteine. The latter is appropriately positioned in the SeMo-active site by a unique VAYRCSFR active site loop. In H. pseudoflava the arginine preceeding the cysteine in the active site loop is modified to a Cγ-hydroxy arginine residue which has no obvious function. The substituents in the first coordination sphere of the Mo-ion are the enedithiolate sulfur atoms of the molybdopterin-cytosine dinucleotide, two oxo- and a sulfido-group. Extended X-ray absorption fine structure spectroscopy (EXAFS), along with the crystal structure of CO dehydrogenase (23.2 U mg−1) at 1.85 Å resolution, have identified a sulfur atom at 2.3 Å from the Mo-ion. The sulfur reacts with cyanide yielding thiocyanate. The corresponding inactive desulfo-CO dehydrogenase shows a typical desulfo inhibited-type of Mo-electron paramagnetic resonance (EPR) spectrum. Structural changes at the SeMo-site during catalysis are suggested by the Mo to Se distance of 3.7 Å and the Mo-S-Se angle of 113° in the oxidized enzyme which increase to 4.1 Å, and 121°, respectively, in the reduced enzyme. The intramolecular electron transport chain in CO dehydrogenase involves the following prosthetic groups and minimal distances: CO → [Mo of the molybdenum cofactor]−14.6Å−[2Fe-2S] I−12.4 Å−[2Fe-2S] II−8.7 Å−[FAD].

About the article

Published Online: 2005-07-05

Published in Print: 2000-09-13


Citation Information: Biological Chemistry, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2000.108.

Export Citation

Citing Articles

Here you can find all Crossref-listed publications in which this article is cited. If you would like to receive automatic email messages as soon as this article is cited in other publications, simply activate the “Citation Alert” on the top of this page.

[1]
Jarett Wilcoxen and Russ Hille
Journal of Biological Chemistry, 2013, Volume 288, Number 50, Page 36052
[2]
Bo Zhang, Craig F. Hemann, and Russ Hille
Journal of Biological Chemistry, 2010, Volume 285, Number 17, Page 12571
[3]
Siyun Xiang, Ying Yao, Yunan Wan, Wangqun Liang, Ruiwei Meng, Qiman Jin, Nannan Wu, Fangyi Xu, Chenjiang Ying, and Xuezhi Zuo
Nutrients, 2016, Volume 8, Number 12, Page 826
[4]
Debarati Paul, Ranjit Kumar, Bindu Nanduri, Todd French, Ken Pendarvis, Ashli Brown, Mark L. Lawrence, Shane C. Burgess, and Stephen Johnson
PLoS ONE, 2011, Volume 6, Number 2, Page e17111
[5]
Raffaella Breglia, Maurizio Bruschi, Ugo Cosentino, Luca De Gioia, Claudio Greco, Toshiko Miyake, and Giorgio Moro
Protein Engineering Design and Selection, 2016
[6]
Hans J. Reich and Robert J. Hondal
ACS Chemical Biology, 2016, Volume 11, Number 4, Page 821
[7]
Marc Birringer, Sandra Pilawa, and Leopold Flohé
Nat. Prod. Rep., 2002, Volume 19, Number 6, Page 693
[9]
Richard A. Rothery and Joel H. Weiner
JBIC Journal of Biological Inorganic Chemistry, 2015, Volume 20, Number 2, Page 349
[10]
Jing Liu, Saumen Chakraborty, Parisa Hosseinzadeh, Yang Yu, Shiliang Tian, Igor Petrik, Ambika Bhagi, and Yi Lu
Chemical Reviews, 2014, Volume 114, Number 8, Page 4366
[11]
Mehmet Can, Fraser A. Armstrong, and Stephen W. Ragsdale
Chemical Reviews, 2014, Volume 114, Number 8, Page 4149
[12]
H. Dobbek, L. Gremer, R. Kiefersauer, R. Huber, and O. Meyer
Proceedings of the National Academy of Sciences, 2002, Volume 99, Number 25, Page 15971
[14]
Jarett Wilcoxen, Bo Zhang, and Russ Hille
Biochemistry, 2011, Volume 50, Number 11, Page 1910
[15]
Keith S. Wong and Walid A. Houry
Journal of Structural Biology, 2012, Volume 179, Number 2, Page 211
[16]
Sven Fuhrmann, Marion Ferner, Thomas Jeffke, Anke Henne, Gerhard Gottschalk, and Ortwin Meyer
Gene, 2003, Volume 322, Page 67
[17]
Karlene K. Gunter, Lisa M. Miller, Michael Aschner, Roman Eliseev, Derrick Depuis, Claire E. Gavin, and Thomas E. Gunter
NeuroToxicology, 2002, Volume 23, Number 2, Page 127
[18]
Stephen W. Ragsdale
Journal of Inorganic Biochemistry, 2007, Volume 101, Number 11-12, Page 1657
[19]
Douglas C. Rees
Annual Review of Biochemistry, 2002, Volume 71, Number 1, Page 221
[20]
Stephen W. Ragsdale
Annals of the New York Academy of Sciences, 2008, Volume 1125, Number 1, Page 129
[22]
Takane Imaoka, Reiko Tanaka, and Kimihisa Yamamoto
Journal of Polymer Science Part A: Polymer Chemistry, 2006, Volume 44, Number 17, Page 5229
[23]
Per E. M. Siegbahn and Alexander F. Shestakov
Journal of Computational Chemistry, 2005, Volume 26, Number 9, Page 888

Comments (0)

Please log in or register to comment.
Log in