title: Orbital contributions to CO oxidation in Mo-Cu carbon monoxide dehydrogenase.
abstract: A molecular orbital analysis provides new insight into the mechanism of Mo/Cu carbon monoxide dehydrogenase, and reveals electronic structure contributions to reactivity that are remarkably similar to the structurally related molybdenum hydroxylases. A calculated reaction barrier of ~12 kcal mol(-1) is in excellent agreement with experiment.
authors: Department of Chemistry and Chemical Biology, The University of New Mexico, MSC03 2060, 1 University of New Mexico, Albuquerque, New Mexico 87131-0001, USA. mkirk@unm.edu.
authors: Benjamin W
authors: BW
authors: Stein
authors: Martin L
authors: ML
authors: Kirk
mesh_terms: D000445:Aldehyde Oxidoreductases / Q000737:chemistry / Q000378:metabolism*; D055162:Biocatalysis; D002248:Carbon Monoxide / Q000737:chemistry / Q000378:metabolism*; D020134:Catalytic Domain; D042621:Comamonadaceae / Q000201:enzymology; D003300:Copper / Q000737:chemistry; D018360:Crystallography, X-Ray; D008968:Molecular Conformation; D008982:Molybdenum / Q000737:chemistry; D009097:Multienzyme Complexes / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D011789:Quantum Theory; D013816:Thermodynamics
chemical_list: D009097:Multienzyme Complexes; D003300:Copper; D002248:Carbon Monoxide; D008982:Molybdenum; D000445:Aldehyde Oxidoreductases; C019823:carbon monoxide dehydrogenase