Molybdenum Site Structure of MOSC Family Proteins
Open Access
- 28 August 2014
- journal article
- research article
- Published by American Chemical Society (ACS) in Inorganic Chemistry
- Vol. 53 (18), 9460-9462
- https://doi.org/10.1021/ic5015863
Abstract
Mo K-edge X-ray absorption spectroscopy has been used to probe as-isolated structures of the MOSC family proteins pmARC-1 and HMCS-CT. The Mo K-edge near-edge spectrum of HMCS-CT is shifted ∼2.5 eV to lower energy compared to the pmARC-1 spectrum, which indicates that as-isolated HMCS-CT is in a more reduced state than pmARC-1. Extended X-ray absorption fine structure analysis indicates significant structural differences between pmARC-1 and HMCS-CT, with the former being a dioxo site and the latter possessing only a single terminal oxo ligand. The number of terminal oxo donors is consistent with pmARC-1 being in the MoVI oxidation state and HMCS-CT in the MoIV state. These structures are in accord with oxygen-atom-transfer reactivity for pmARC-1 and persulfide bond cleavage chemistry for HMCS-CT.Keywords
Funding Information
- National Institute of General Medical Sciences (GM 057378)
- Deutsche Forschungsgemeinschaft (Bi 1075/2-2)
This publication has 28 references indexed in Scilit:
- Identification of persulfide-binding and disulfide-forming cysteine residues in the NifS-like domain of the molybdenum cofactor sulfurase ABA3 by cysteine-scanning mutagenesisBiochemical Journal, 2012
- Molybdenum enzymes in higher organismsCoordination Chemistry Reviews, 2011
- Biochemical and Spectroscopic Characterization of the Human Mitochondrial Amidoxime Reducing Components hmARC-1 and hmARC-2 Suggests the Existence of a New Molybdenum Enzyme Family in EukaryotesPublished by Elsevier BV ,2010
- Reduction ofN-Hydroxy-sulfonamides, IncludingN-Hydroxy-valdecoxib, by the Molybdenum-Containing Enzyme mARCDrug Metabolism and Disposition, 2010
- Evolutionary Persistence of the Molybdopyranopterin-Containing Sulfite Oxidase Protein FoldMicrobiology and Molecular Biology Reviews, 2008
- Binding of Sulfurated Molybdenum Cofactor to the C-terminal Domain of ABA3 from Arabidopsis thaliana Provides Insight into the Mechanism of Molybdenum Cofactor SulfurationPublished by Elsevier BV ,2008
- Heterodimeric nitrate reductase (NapAB) fromCupriavidus necatorH16: purification, crystallization and preliminary X-ray analysisActa Crystallographica Section F Structural Biology and Crystallization Communications, 2007
- Reduction of sulfamethoxazole and dapsone hydroxylamines by a microsomal enzyme system purified from pig liver and pig and human liver microsomesLife Sciences, 2005
- Molybdenum sites of sulfite oxidase and xanthine dehydrogenase. A comparison by EXAFSJournal of the American Chemical Society, 1981
- Single-crystal polarized x-ray absorption spectroscopy. Observation and theory for thiomolybdate(2-)Journal of the American Chemical Society, 1981