Structure/function relationships in nickel metallobiochemistry

Current Opinion in Chemical Biology

Volumn 3, Issue 2, 1999, Pages 188-199

  Maroney, Michael J ^a  

^a UNIVERSITY OF MASSACHUSETTS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ACETYL COENZYME A SYNTHETASE; CARBON MONOXIDE DEHYDROGENASE; HYDROGENASE; ISOMERASE; LACTOYLGLUTATHIONE LYASE; METALLOPROTEIN; NICKEL; NICKEL COMPLEX; SUPEROXIDE DISMUTASE; UREASE;

BIOCHEMISTRY; ESCHERICHIA COLI; OXIDATION REDUCTION REACTION; REVIEW; STREPTOMYCES; STRUCTURE ACTIVITY RELATION;

ESCHERICHIA COLI; STREPTOMYCES; STREPTOMYCES SEOULENSIS;

EID: 0033120016     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(99)80032-5     Document Type: Article

References (88)

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70. 4] cluster involved in CO oxidation (Cluster C). This provides support for mechanisms that involve CO binding to Ni and attack by Fe-bound hydroxide. In addition, evidence that Cluster C has a histidine Fe ligand is also provided.
71. 4 clusters. A potential role in the construction of cluster C was proposed.
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73. red-CO.
74. 4 cube. The properties of two populations of the cluster (labile versus nonlabile nickel) were examined. Differences in the redox and structural properties of the two sites were identified.
75. 2-dependent conformational change affecting the properties of all three clusters in both subunits.
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77. 2-type nucleophilic displacement reactions and do not involve radical chem.
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79. 430) in two distinct forms. In one form, the Ni tetrapyrrole is ligated by (H)S-CoM via the S-donor. In the second form, the product heterodisulfide formed between CoM and CoB is ligated to the Ni via the CoM sulfonate group.
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81. 430. Struct Bonding 1998, 91:31-63.
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83. 430 by the compensated ROESY experiment. Bull Kor Chem Soc 1998, 19:379-383.
84. Becker DF, Ragsdale SW: Activation of methyl-SCoM reductase to high specific activity after treatment of whole cells with sodium sulfide. Biochemistry 1998, 37:2639-2647. This paper reports on a method for producing highly active samples of methylcoenzyme M reductase. The method, which involves treatment of cells with sodium sulfide, yields enzyme that contains labeled sulfur atoms, suggesting that the added sulfur is involved in ligating Ni. In contrast, oxidized sulfur in the form of sulfite gave states of the enzyme that are not readily activated. The paper points to the redox role played by sulfur ligands in generating active enzyme.
85. 430 is reduced to the formal Ni(I) oxidation state and provides a preparation for highly active enzyme.
86. 430. Met Ions Biol Syst 1993, 29:287-337.
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