Cytochrome c peroxidase from Methylococcus capsulatus Bath |
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| Authors: | James A. Zahn David M. Arciero A. B. Hooper Joel R. Coats A. A. DiSpirito |
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| Affiliation: | (1) Department of Microbiology, Immunology, and Preventive Medicine, Iowa State University, 207 Science Building I, Ames, IA 50011-3211, USA Tel. +1-515-294-2944; Fax +1-515-294-6019 e-mail: aland@iastate.edu, US;(2) Graduate Program in Toxicology, Iowa State University, Ames, IA 50011, USA, US;(3) Graduate Programs in Biochemistry and Microbiology, University of Minnesota, St. Paul, Minnesota 55108, USA, US;(4) Department of Entomology Iowa State University, Ames, Iowa 50011, USA, US |
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| Abstract: | A bacterial cytochrome c peroxidase was purified from the obligate methanotroph Methylococcus capsulatus Bath in either the fully oxidized or the half reduced form depending on the purification procedure. The cytochrome was a homo-dimer with a subunit mol mass of 35.8 kDa and an isoelectric point of 4.5. At physiological temperatures, the enzyme contained one high-spin, low-potential (E m7 = –254 mV) and one low-spin, high-potential (E m7 = +432 mM ) heme. The low-potential heme center exhibited a spin-state transition from the penta-coordinated, high-spin configuration to a low-spin configuration upon cooling the enzyme to cryogenic temperatures. Using M. capsulatus Bath ferrocytochrome c 555 as the electron donor, the K M and V max for peroxide reduction were 510 ± 100 nM and 425 ± 22 mol ferrocytochrome c 555 oxidized min–1 (mole cytochrome c peroxidase)–1, respectively. Received: 6 January 1997 / Accepted: 27 May 1997 |
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| Keywords: | Methanotroph Methylotroph Cytochrome c peroxidase Cytochrome aa3 Methylamine oxidation Methanol oxidation moxG |
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