Publication Date:
1997-02-28
Description:
Formate dehydrogenase H from Escherichia coli contains selenocysteine (SeCys), molybdenum, two molybdopterin guanine dinucleotide (MGD) cofactors, and an Fe4S4 cluster at the active site and catalyzes the two-electron oxidation of formate to carbon dioxide. The crystal structures of the oxidized [Mo(VI), Fe4S4(ox)] form of formate dehydrogenase H (with and without bound inhibitor) and the reduced [Mo(IV), Fe4S4(red)] form have been determined, revealing a four-domain alphabeta structure with the molybdenum directly coordinated to selenium and both MGD cofactors. These structures suggest a reaction mechanism that directly involves SeCys140 and His141 in proton abstraction and the molybdenum, molybdopterin, Lys44, and the Fe4S4 cluster in electron transfer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boyington, J C -- Gladyshev, V N -- Khangulov, S V -- Stadtman, T C -- Sun, P D -- New York, N.Y. -- Science. 1997 Feb 28;275(5304):1305-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Structure, National Institute of Allergy and Infectious Diseases, National Institutes of Health (NIH), Rockville, MD 20852, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/9036855" target="_blank"〉PubMed〈/a〉
Keywords:
Binding Sites
;
Carbon Dioxide/metabolism
;
Catalysis
;
Crystallography, X-Ray
;
Electron Transport
;
Escherichia coli/enzymology
;
Ferrous Compounds/*chemistry
;
Formate Dehydrogenases/*chemistry/metabolism
;
Formates/*metabolism
;
Guanine Nucleotides/chemistry/metabolism
;
Hydrogen Bonding
;
Hydrogenase/*chemistry/metabolism
;
Ligands
;
Models, Molecular
;
Molecular Sequence Data
;
Molybdenum/chemistry/metabolism
;
Multienzyme Complexes/*chemistry/metabolism
;
Nitrites/chemistry
;
Oxidation-Reduction
;
*Protein Conformation
;
Protein Structure, Secondary
;
Protein Structure, Tertiary
;
Protons
;
Pterins/chemistry/metabolism
;
Selenocysteine/chemistry/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
