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1
Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath).荚膜甲基球菌（巴斯德菌株）甲烷单加氧酶的黄素酶NADH-受体还原酶（组分C）的第二个辅基的表征
Biochem J. 1979 Mar 1;177(3):903-8. doi: 10.1042/bj1770903.
2
Further characterisation of the FAD and Fe2S2 redox centres of component C, the NADH:acceptor reductase of the soluble methane monooxygenase of Methylococcus capsulatus (Bath).荚膜甲基球菌（巴斯德菌）可溶性甲烷单加氧酶的组分C（NADH：受体还原酶）的FAD和Fe2S2氧化还原中心的进一步表征
Eur J Biochem. 1985 Mar 1;147(2):291-6. doi: 10.1111/j.1432-1033.1985.tb08749.x.
3
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4
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5
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6
Methane monooxygenase: purification and properties of flavoprotein component.甲烷单加氧酶：黄素蛋白组分的纯化及性质
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7
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8
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9
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The membrane-associated form of methane mono-oxygenase from Methylococcus capsulatus (Bath) is a copper/iron protein.来自荚膜甲基球菌（巴斯）的膜结合型甲烷单加氧酶是一种铜/铁蛋白。
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1
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Appl Environ Microbiol. 1985 May;49(5):1282-9. doi: 10.1128/aem.49.5.1282-1289.1985.
6
Microbial Oxidation of Hydrocarbons: Properties of a Soluble Methane Monooxygenase from a Facultative Methane-Utilizing Organism, Methylobacterium sp. Strain CRL-26.微生物烃类氧化：一种兼性利用甲烷生物体甲基杆菌菌株 CRL-26 的可溶性甲烷单加氧酶的性质。
Appl Environ Microbiol. 1982 Nov;44(5):1130-7. doi: 10.1128/aem.44.5.1130-1137.1982.
7
The Leeuwenhoek Lecture 2000 the natural and unnatural history of methane-oxidizing bacteria.2000年列文虎克讲座：甲烷氧化菌的自然与非自然历史。
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Soluble methane monooxygenase gene clusters from trichloroethylene-degrading Methylomonas sp. strains and detection of methanotrophs during in situ bioremediation.来自三氯乙烯降解甲基单胞菌属菌株的可溶性甲烷单加氧酶基因簇及原位生物修复过程中甲烷营养菌的检测
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9
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本文引用的文献

1
THE CONTENT AND POSSIBLE CATALYTIC SIGNIFICANCE OF LABILE SULFIDE IN SOME METALLOFLAVOPROTEINS.某些金属黄素蛋白中不稳定硫化物的含量及其可能的催化意义
J Biol Chem. 1965 May;240:2222-8.
2
Enzymes of the mandelate pathway in Bacterium N.C.I.B. 8250.细菌N.C.I.B. 8250中扁桃酸途径的酶
Biochem J. 1968 Apr;107(4):497-506. doi: 10.1042/bj1070497.
3
The direct linear plot. A new graphical procedure for estimating enzyme kinetic parameters.直接线性作图法。一种用于估算酶动力学参数的新的图形方法。
Biochem J. 1974 Jun;139(3):715-20. doi: 10.1042/bj1390715.
4
Iron-sulfur proteins: structure and function.铁硫蛋白：结构与功能
Annu Rev Biochem. 1973;42(0):159-204. doi: 10.1146/annurev.bi.42.070173.001111.
5
Spin-spin interaction between molybdenum and one of the iron-sulphur systems of xanthine oxidase and its relevance to the enzymic mechanism.钼与黄嘌呤氧化酶的铁硫系统之一之间的自旋-自旋相互作用及其与酶促机制的相关性。
Biochem J. 1972 Nov;130(1):239-49. doi: 10.1042/bj1300239.
6
Letter: Extrusion of Fe2S2 and Fe4S4 cores from the active sites of ferredoxin proteins.信函：Fe2S2和Fe4S4核心从铁氧化还原蛋白的活性位点挤出。
J Am Chem Soc. 1975 Jan 22;97(2):463-4. doi: 10.1021/ja00835a064.
7
Some properties of a soluble methane mono-oxygenase from Methylococcus capsulatus strain Bath.来自荚膜甲基球菌巴斯菌株的一种可溶性甲烷单加氧酶的某些特性。
Biochem J. 1976 Aug 1;157(2):495-7. doi: 10.1042/bj1570495.
8
Iron-sulfur clusters and cysteine distribution in a ferredoxin from Azotobacter vinelandii.维涅兰德固氮菌铁氧化还原蛋白中的铁硫簇和半胱氨酸分布
Biochem Biophys Res Commun. 1976 May 17;70(2):582-8. doi: 10.1016/0006-291x(76)91087-1.
9
Inhibition of methylene blue formation during determination of the acid-labile sulfide of iron-sulfur protein samples containing dithionite.在测定含有连二亚硫酸盐的铁硫蛋白样品的酸不稳定硫化物过程中对亚甲蓝形成的抑制作用。
Anal Biochem. 1977 May 1;79(1-2):157-65. doi: 10.1016/0003-2697(77)90390-6.
10
Quantitative extrusions of the Fe4S4 cores of the active sites of ferredoxins and the hydrogenase of Clostridium pasteurianum.嗜热栖热放线菌铁氧化还原蛋白活性位点的Fe4S4核心和氢化酶的定量挤压。
J Am Chem Soc. 1977 Jan 19;99(2):584-95. doi: 10.1021/ja00444a044.

荚膜甲基球菌（巴斯德菌株）甲烷单加氧酶的黄素酶NADH-受体还原酶（组分C）的第二个辅基的表征

Characterization of the second prosthetic group of the flavoenzyme NADH-acceptor reductase (component C) of the methane mono-oxygenase from Methylococcus capsulatus (Bath).

作者信息

Colby J, Dalton H

出版信息

Biochem J. 1979 Mar 1;177(3):903-8. doi: 10.1042/bj1770903.

DOI:10.1042/bj1770903
PMID:220953
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC1186456/
Abstract
  1. A new two-step purification is described that routinely yields 100mg quantities of component C for biochemical studies. 2. Chemical analyses show component C purified by this procedure to contain 2 g-atoms of iron, 2 mol of acid-labile sulphide (S) and 1 mol of FAD per mol of protein. 3. The Fe-S core of component C was extruded by treating the protein with p-methoxybenzenethiol in hexamethyl phosphoramide/50mM-Tris/HCl buffer, pH 8.5 (4:1, v/v), under anaerobic conditions. The spectral properties of the extruded core suggest that component C contains 1 mol of [2Fe-2S(S-Cys)4] centre per mol of protein. 4. E.p.r. spectroscopy confirms the presence of a Fe-S centre in component C. 5. Component C catalyses the reduction by NADH of ferricyanide, 2,6-dichlorophenol-indophenol or horse heart cytochrome c, with specific activities of 50--230 units/mg of protein. 6. The optimum pH for the NADH-acceptor reductase activity is 8.5--9.0, and the apparent Km values for NADH and NADPH are 0.05mM and 15.5mM respectively. 7. Unlike methane mono-oxygenase activity, NADH-acceptor reductase activity of component C is not inhibited by 8-hydroxyquinoline or by acetylene.
摘要
  1. 本文描述了一种新的两步纯化方法，该方法常规可获得100毫克用于生化研究的组分C。2. 化学分析表明，通过此方法纯化的组分C每摩尔蛋白质含有2克原子铁、2摩尔酸不稳定硫化物（S）和1摩尔黄素腺嘌呤二核苷酸（FAD）。3. 在厌氧条件下，于六甲基磷酰胺/50mM - 三羟甲基氨基甲烷/盐酸缓冲液（pH 8.5，4:1，v/v）中，用对甲氧基苯硫酚处理蛋白质，可挤出组分C的铁硫核心。挤出核心的光谱特性表明，组分C每摩尔蛋白质含有1摩尔[2Fe - 2S（S - 半胱氨酸）4]中心。4. 电子顺磁共振光谱证实了组分C中存在铁硫中心。5. 组分C催化烟酰胺腺嘌呤二核苷酸（NADH）还原铁氰化物、2,6 - 二氯酚靛酚或马心细胞色素c，比活性为50 - 230单位/毫克蛋白质。6. NADH - 受体还原酶活性的最适pH为8.5 - 9.0，NADH和烟酰胺腺嘌呤二核苷酸磷酸（NADPH）的表观米氏常数（Km）值分别为0.05mM和15.5mM。7. 与甲烷单加氧酶活性不同，组分C的NADH - 受体还原酶活性不受8 - 羟基喹啉或乙炔抑制。