about
Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzymeSubstrate Orientation and Catalysis at the Molybdenum Site in Xanthine Oxidase: CRYSTAL STRUCTURES IN COMPLEX WITH XANTHINE AND LUMAZINEStructure of a hyperthermophilic tungstopterin enzyme, aldehyde ferredoxin oxidoreductaseMicrobial Metabolism of Quinoline and Related Compounds. XVIII. Purification and Some Properties of the Molybdenum- and Iron-Containing Quinaldic acid 4-oxidoreductase fromSerratia marcescens2CC-1The four aldehyde oxidases of Drosophila melanogaster have different gene expression patterns and enzyme substrate specificitiesElucidating the catalytic mechanism of sulfite oxidizing enzymes using structural, spectroscopic, and kinetic analyses.Molybdenum: an essential trace element.Characterization of crystalline formate dehydrogenase H from Escherichia coli. Stabilization, EPR spectroscopy, and preliminary crystallographic analysis.HIGH-RESOLUTION EPR SPECTROSCOPY OF MO ENZYMES. SULFITE OXIDASES: STRUCTURAL AND FUNCTIONAL IMPLICATIONS.Implications for the mechanism of sulfite oxidizing enzymes from pulsed EPR spectroscopy and DFT calculations for "difficult" nuclei.Coordination of selenium to molybdenum in formate dehydrogenase H from Escherichia coliIdentity of the exchangeable sulfur-containing ligand at the Mo(V) center of R160Q human sulfite oxidaseMolybdenum(VI) salts convert the xanthine oxidoreductase apoprotein into the active enzyme in mouse L929 fibroblastic cells.A structure-based catalytic mechanism for the xanthine oxidase family of molybdenum enzymes.Molybdenum-containing nitrite reductases: Spectroscopic characterization and redox mechanism.Investigation of the redox centres of periplasmic selenate reductase from Thauera selenatis by EPR spectroscopy.Isolation, in the intact state, of the pterin molybdenum cofactor from xanthine oxidase.Information from e.p.r. spectroscopy on the iron-sulphur centres of the iron-molybdenum protein (aldehyde oxidoreductase) of Desulfovibrio gigas.The nature of the phosphate complex of sulphite oxidase from electron-paramagnetic-resonance studies.The isolation of demolybdo xanthine oxidase from bovine milk.Use of rosy mutant strains of Drosophila melanogaster to probe the structure and function of xanthine dehydrogenase.X-ray-absorption and electron-paramagnetic-resonance spectroscopic studies of the environment of molybdenum in high-pH and low-pH forms of Escherichia coli nitrate reductase.Purification and characterization of the assimilatory nitrate reductase of Azotobacter vinelandii.Identification of periplasmic nitrate reductase Mo(V) EPR signals in intact cells of Paracoccus denitrificans.Information from e.x.a.f.s. spectroscopy on the structures of different forms of molybdenum in xanthine oxidase and the catalytic mechanism of the enzyme.Structural investigation of the molybdenum site of the periplasmic nitrate reductase from Thiosphaera pantotropha by X-ray absorption spectroscopy.Redox centers of 4-hydroxybenzoyl-CoA reductase, a member of the xanthine oxidase family of molybdenum-containing enzymes.
P2860
Q24562159-C063C6A5-F862-43D5-BD73-0D69D31A5747Q27653276-E46EB638-313B-44CD-8714-26B7C66CA27DQ27730392-4AC05DEF-E606-4AD9-A9E6-A7D920ECD491Q29399548-40FE920F-4448-428F-8E64-B8F803809FDEQ33746582-E5DA5A95-1943-40D6-83AB-747A4285039BQ34082032-96F1E381-BADA-4DC6-8347-28F0902C231DQ34349198-251BC180-1922-417E-B284-C0E8A83BC903Q34378846-DD42FE14-F7BD-4EF5-8CE0-6B5BDFD6D61DQ34539174-B744E9E4-E270-402A-80A2-068B1DB39F88Q34814682-EB548DED-81B5-495E-9AAC-A47130B257C3Q35659557-94286ACF-D7E9-49AD-B1FB-50A2E30D24C8Q35740312-70718C44-ED54-4443-AA8B-E89549A9E8A4Q36744795-4B7B523A-E467-4FAA-B74A-9DE90929B48EQ37374418-224BF7A3-F90C-4611-8F42-182EEE213D83Q38816387-732B0D47-F1B5-42AD-9057-DA6225D7AA03Q39254921-A9EF2F15-8DD7-4A3B-A8C3-0DD30EAE94A0Q41942883-0A840C07-302D-4A95-97CC-0494E6112017Q41997128-BC5890BD-6FE6-40D3-8D89-B98DA81B31B4Q42133326-E12915F2-4EF1-45A7-9FCC-FA696A647417Q42146306-5BAB02F9-34BE-44C0-B865-5EE2DA007573Q42258579-78845FDB-AB83-43E8-9662-D2B9B3986C09Q42679915-0A48FD18-4F51-4A8D-AF76-EA8DFE62CC95Q42796511-0E2DA1B6-94AA-4599-B254-5FC46121CB95Q42821802-A3A5272E-14A4-414F-B94D-7561DFA37E10Q42836348-EE7A727F-70DE-4458-A824-880CDD41AC61Q42983057-F03E5D84-5ED7-44E8-8C42-350680493CD3Q43767940-6590F78F-0EE1-446B-AB23-038FD13F9820
P2860
description
1988 nî lūn-bûn
@nan
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
1988年论文
@zh
1988年论文
@zh-cn
name
The inorganic biochemistry of molybdoenzymes.
@en
The inorganic biochemistry of molybdoenzymes.
@nl
type
label
The inorganic biochemistry of molybdoenzymes.
@en
The inorganic biochemistry of molybdoenzymes.
@nl
prefLabel
The inorganic biochemistry of molybdoenzymes.
@en
The inorganic biochemistry of molybdoenzymes.
@nl
P2860
P1476
The inorganic biochemistry of molybdoenzymes.
@en
P2093
P2860
P304
P356
10.1017/S0033583500004479
P577
1988-08-01T00:00:00Z