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Volumn 27, Issue 7, 2002, Pages 360-367

Molybdenum and tungsten in biology

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE; DIMETHYL SULFOXIDE REDUCTASE; ENZYME; FERREDOXIN; FORMATE DEHYDROGENASE; MOLYBDENUM; OXIDOREDUCTASE; PTERIN; SULFITE OXIDASE; TUNGSTEN; XANTHINE OXIDASE; ALDEHYDE DEHYDROGENASE; BACTERIAL PROTEIN; IRON SULFUR PROTEIN; METALLOPROTEIN; MOLYBDENUM COFACTOR; PTERIDINE DERIVATIVE;

EID: 0036629252     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(02)02107-2     Document Type: Review
Times cited : (383)

References (53)
  • 1
    • 0011509370 scopus 로고    scopus 로고
    • Structural and functional aspects of metal sites in biology
    • (1996) Chem. Rev. , vol.96 , pp. 2239-2314
    • Holm, R.H.1
  • 6
    • 0020083365 scopus 로고
    • Chemical and spectral properties of carbon monoxide:methylene blue reductase. The molybdenum-containing iron-sulfur flavoprotein from Pseudomonas carboxydovorans
    • (1995) J. Biol. Chem. , vol.257 , pp. 1333-1341
    • Meyer, O.1
  • 7
    • 0030006891 scopus 로고    scopus 로고
    • Crystal structure of DMSO reductase: Redox-linked changes in molybdeopterin coordination
    • (1996) Science , vol.272 , pp. 1615-1621
    • Schindelin, H.1
  • 8
    • 0003123613 scopus 로고    scopus 로고
    • Crystal structure of the first dissimilatory nitrate reductase at 1.9 Å solved by MAD methods
    • (1999) Structure , vol.7 , pp. 65-79
    • Dias, J.M.1
  • 9
    • 0031043109 scopus 로고    scopus 로고
    • Crystal structure of formate dehydrogenase H: Catalysis involving Mo, molybdopterin, selenocysteine and an Fe4S4 cluster
    • (1997) Science , vol.275 , pp. 1305-1308
    • Boyington, J.C.1
  • 10
    • 0035095129 scopus 로고    scopus 로고
    • Crystal structure of the 100 kDa arsenite oxidase from Alcaligenes faecalis in two crystal forms at 1.64 and 2.03 Å
    • (2001) Structure , vol.9 , pp. 125-132
    • Ellis, P.1
  • 11
    • 0026550359 scopus 로고
    • Cloning and nucleotide sequence of the psrA gene of Wolinella succinogenes polysulfide reductase
    • (1992) Eur. J. Biochem. , vol.206 , pp. 503-510
    • Krafft, T.1
  • 13
    • 0033605085 scopus 로고    scopus 로고
    • Formaldehyde ferredoxin oxidoreductase from Pyrococcus furiosus. The 1.85 Å resolution crystal structure and its mechanistic implications
    • (1999) J. Mol. Biol. , vol.286 , pp. 899-914
    • Hu, Y.1
  • 14
    • 0028838798 scopus 로고
    • Purification and characterization of acetylene hydratase of Pelobacter acetylenicus, a tungsten iron-sulfur protein
    • (1995) J. Bacteriol. , vol.177 , pp. 5767-5772
    • Rosner, B.M.1    Schink, B.2
  • 15
    • 0028961901 scopus 로고
    • Structure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductase
    • (1995) Science , vol.267 , pp. 1463-1469
    • Chan, M.K.1
  • 17
    • 0028807552 scopus 로고
    • Crystal structure of the xanthine oxidase-related aldehyde oxido-reductase from D. Gigas
    • (1995) Science , vol.270 , pp. 1170-1176
    • Romão, M.J.1
  • 20
    • 0031459478 scopus 로고    scopus 로고
    • Molecular basis of sulfite oxidase deficiency from the structure of sulfite oxidase
    • (1997) Cell , vol.91 , pp. 973-983
    • Kisker, C.1
  • 21
    • 0029075043 scopus 로고
    • Structural studies on corn nitrate reductase: Refined structure of the cytochrome b reductase fragment at 2.5 Å, its ADP complex and an active-site mutant and modeling of the cytochrome b domain
    • (1995) J. Mol. Biol. , vol.248 , pp. 931-948
    • Lu, G.1
  • 22
    • 0030592449 scopus 로고    scopus 로고
    • Crystal structure of dimethyl sulfoxide reductase from Rhodobacter capsulatus at 1.88 Å resolution
    • (1996) J. Mol Biol. , vol.263 , pp. 53-69
    • Schneider, F.1
  • 23
    • 0026800924 scopus 로고
    • Molecular analysis of dimethyl sulfoxide reductase: A complex iron-sulfur molybdoenzyme of Escherichia coli
    • (1992) Biochim. Biophys. Acta , vol.1102 , pp. 1-18
    • Weiner, J.H.1
  • 25
    • 0029816512 scopus 로고    scopus 로고
    • The molybdenum center of sulfite oxidase: A comparison of wild-type and the cysteine 207 to serine mutant using X-ray absorption spectroscopy
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8588-8592
    • George, G.N.1
  • 26
    • 33845558282 scopus 로고
    • Molybdenum sites of sulfite oxidase and xanthine dehydrogenase. A comparison by EXAFS
    • (1981) J. Am. Chem. Soc. , vol.103 , pp. 7721-7727
    • Cramer, S.P.1
  • 27
    • 0033538063 scopus 로고    scopus 로고
    • Characterization of DorC from Rhodobacter capsulatus, a c-type cytochrome involved in electron transfer to dimethyl sulfoxide reductase
    • (1999) J. Biol. Chem. , vol.274 , pp. 9911-9914
    • Shaw, A.L.1
  • 28
    • 0034674980 scopus 로고    scopus 로고
    • The 1.3 Å structure of Rhodobacter sphaeroides dimethyl sulfoxide reductase reveals two distinct molybdenum coordination environments
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 7673-7680
    • Li, H.-K.1
  • 29
    • 0031593019 scopus 로고    scopus 로고
    • Active site structures and catalytic mechanism of Rhodobacter sphaeroides dimethyl sulfoxide reductase as revealed by resonance Raman spectroscopy
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 12906-12916
    • Garton, S.D.1
  • 30
    • 0029159268 scopus 로고
    • Direct oxygen atom transfer in the mechanism of action of Rhodobacter sphaeroides dimethylsulfoxide reductase
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 827-828
    • Schultz, B.E.1
  • 31
    • 0033614820 scopus 로고    scopus 로고
    • Reactions of dimethylsulfoxide reductase from Rhodobacter capsulatus with dimethyl sulfide and dimethyl sulfoxide: Complexities revealed by conventional and stopped-flow spectrophotometry
    • (1999) Biochemistry , vol.38 , pp. 8501-8511
    • Adams, B.1
  • 32
  • 33
    • 0035819941 scopus 로고    scopus 로고
    • Bis(dithiolene)molybdenum analogues relevant to the DMSO reductase enzyme family: Synthesis, structures and oxygen atom transfer reaction and kinetics
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1920-1930
    • Lim, B.S.1    Holm, R.H.2
  • 34
    • 0035819949 scopus 로고    scopus 로고
    • Oxo transfer reactions mediated by bis(dithiolene)tungsten analogues of the active sites of molybdoenzymes in the DMSO reductase family: Comparative reactivity of tungsten and molybdenum
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 1931-1943
    • Sung, K.-M.1    Holm, R.H.2
  • 35
    • 0034805672 scopus 로고    scopus 로고
    • The theoretical transition state structure of a model complex bears a striking resemblance to the active site structure of DMSO reductase
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 5820-5821
    • Webster, C.E.1    Hall, M.B.2
  • 36
    • 0014028028 scopus 로고
    • Catalysis of the direct transfer of oxygen from nicotinamide N-oxide to xanthine by xanthine oxidase
    • (1966) J. Biol. Chem. , vol.241 , pp. 4798-4801
    • Murray, K.N.1
  • 38
    • 0030022686 scopus 로고    scopus 로고
    • Evidence favoring molybdenum-carbon bond formation in xanthine oxidase action: 17O- and 13C-ENDOR and kinetic studies
    • (1996) Biochemistry , vol.35 , pp. 1432-1443
    • Howes, B.D.1
  • 40
    • 0000842697 scopus 로고
    • Molybdenum(V) sites in xanthine oxidase and relevant analog complexes: Comparison of oxygen-17 hyperfine coupling
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 5385-5392
    • Greenwood, R.J.1
  • 42
    • 0026322388 scopus 로고
    • The reductive half-reaction of xanthine oxidase. Spectral intermediates in the hydroxylation of 2-hydroxy-6-methylpurine
    • (1991) J. Biol. Chem. , vol.266 , pp. 23724-23731
    • McWhirter, R.B.1    Hille, R.2
  • 43
    • 0027964394 scopus 로고
    • Kinetics and thermodynamics of the molecular mechanism of the reductive half-reaction of xanthine oxidase
    • (1994) Biochemistry , vol.33 , pp. 10305-10312
    • Mondal, M.S.1    Mitra, S.2
  • 44
  • 45
    • 77956942930 scopus 로고
    • Molybdenum iron-sulfur flavin hydroxylases and related enzymes
    • P.D. Boyer. Academic Press
    • (1975) The Enzymes , vol.12 , pp. 299-419
    • Bray, R.C.1
  • 47
    • 0036153761 scopus 로고    scopus 로고
    • Crystal structures of the active and alloxanthine-inhibited forms of xanthine dehydrogenase from Rhodobacter capsulatus
    • (2002) Structure , vol.10 , pp. 115-125
    • Truglio, J.1
  • 48
    • 0030988323 scopus 로고    scopus 로고
    • Prediction of alternative structures of the molybdenum site in the xanthine oxidase-related aldehyde oxido reductase
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3159-3160
    • Voityuk, A.A.1
  • 49
    • 0001136357 scopus 로고    scopus 로고
    • Substrate oxidation in the active site of xanthine oxidase and related enzymes. A model density functional study
    • (1998) Inorg. Chem. , vol.37 , pp. 176-180
    • Voityuk, A.A.1
  • 50
    • 0000269665 scopus 로고    scopus 로고
    • The mechanism of formamide hydroxylation catalyzed by a molybdenum-dithiolene complex: A model for xanthine oxidase reactivity
    • (1999) J. Phys. Chem. , vol.103 , pp. 5406-5412
    • Ilich, P.1    Hille, R.2
  • 52
    • 0034788571 scopus 로고    scopus 로고
    • A theoretical study of the primary oxo transfer reaction of a dioxo molybdenum(VI) compound with imine thiolate chelating ligands: A molybdenum oxotransferase analogue
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3995-4002
    • Thomson, L.M.1    Hall, M.B.2
  • 53
    • 0035918138 scopus 로고    scopus 로고
    • An active site tyrosine influences the ability of the dimethyl sulfoxide reductase family of molybdopterin enzymes to reduce S-oxides
    • (2001) J. Biol. Chem. , vol.276 , pp. 13178-13185
    • Johnson, K.E.1    Rajagopalan, K.V.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.