1990
DOI: 10.1016/0076-6879(90)88033-7
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[31] Methane monooxygenase from Methylosinus trichosporium OB3b

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Cited by 137 publications
(136 citation statements)
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“…The growth of M. trichosporium OB3b and purification of MMOH and MMOB were as reported previously (Fox et al, 1989(Fox et al, , 1990a. The specific activity at 23 "C of MMOB was 7,000 nmol/min/mg.…”
Section: Crystal Formmentioning
confidence: 79%
See 1 more Smart Citation
“…The growth of M. trichosporium OB3b and purification of MMOH and MMOB were as reported previously (Fox et al, 1989(Fox et al, , 1990a. The specific activity at 23 "C of MMOB was 7,000 nmol/min/mg.…”
Section: Crystal Formmentioning
confidence: 79%
“…MMO exists in both a soluble (sMMO) and a particulate (pMMO) form (Dalton, 1980;Anthony, 1982). sMMO has been purified and characterized from the Type X methanotroph, Methylococcus capsulatus Bath (MMO Bath) (Dalton, 1980, 199 Dalton, 1984;Pilkington & Dalton, 1990), and several Type I1 methanotrophs including, Methylosinus trichosporium 0B3b (MMO OB3b) (Fox et al, 1989(Fox et al, , 1990a, and Methylobacterium sp. CRL-26 (Patel & Savas, 1987).…”
mentioning
confidence: 99%
“…Although the soluble MMO (sMMO) system is expressed by only a few organisms under low copper conditions (3), it has been characterized far more extensively than the particulate form because of difficulties purifying and stabilizing the particulate MMO enzymes (4 -6). The sMMO proteins from two methanotrophic bacteria, Methylococcus capsulatus (Bath) (7,8) and Methylosinus trichosporium OB3b (9,10), have been studied in great detail (11)(12)(13)(14)(15)(16)(17)(18)(19). Both systems require three components: a dimeric (␣␤␥) 2 hydroxylase (MMOH, 251 kDa) with dinuclear, carboxylate-bridged iron centers, where dioxygen activation and methane hydroxylation occur; a regulatory protein (MMOB, 15.9 kDa); and a reductase (MMOR, 38.5 kDa) that transfers electrons from NADH to the MMOH diiron sites, thereby priming the hydroxylase for reaction with dioxygen.…”
mentioning
confidence: 99%
“…The enzyme consists of three components : the hydroxylase, the reductase and a regulatory protein, component B. The p-OH bridged diiron site [3, 41 resides in the hydroxylase and it is the fully reduced, Fe(II)Fe(II), form which is catalytically active [5]. …”
mentioning
confidence: 99%