Oxygen activating nonheme iron enzymes

Current Opinion in Chemical Biology

Volumn 2, Issue 2, 1998, Pages 159-172

  Lange, Steven J ^a   Que Jr , Lawrence ^a  

^a UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PSEUDOMONAS; PSEUDOMONAS OLEOVORANS; XANTHOBACTER;

ACYL (ACYL CARRIER PROTEIN)DESATURASE; ACYL-(ACYL-CARRIER-PROTEIN)DESATURASE; BACTERIAL PROTEIN; HISTIDINE; ISOPENICILLIN N SYNTHETASE; METHANE MONOOXYGENASE; MIXED FUNCTION OXIDASE; NONHEME IRON PROTEIN; OXIDOREDUCTASE; OXYGENASE; PROTOCATECHUATE 3,4 DIOXYGENASE; RIBONUCLEOTIDE REDUCTASE;

BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; PHYSIOLOGY; REVIEW;

BACTERIAL PROTEINS; BINDING SITES; HISTIDINE; MIXED FUNCTION OXYGENASES; MODELS, MOLECULAR; NONHEME IRON PROTEINS; OXIDOREDUCTASES; OXYGENASES; PROTOCATECHUATE-3,4-DIOXYGENASE; RIBONUCLEOTIDE REDUCTASES;

EID: 0032039677     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80057-4     Document Type: Article

References (90)

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81. 2 as oxidant.
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88. 2 via a common mechanism.
89. x, which has Mössbauer properties similar to ribonucleotide reductase R2 protein (RNR R2) X intermediate (RNR R2-X). This observation supports the hypothesis that MMOH-Q and RNR R2 have similar structures.
90. 2 core that can serve as a basis for interpreting Raman data on MMOH-Q and RNR R2-X.