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The structure of adrenodoxin reductase of mitochondrial P450 systems: Electron transfer for steroid biosynthesis
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Adrenodoxin reductase is involved in the biosynthesis of all steroid hormones. The structure provides an insight into the electron transduction pathway in which adrenodoxin reductase recieves two electrons from NADPH and passes them to adrenodoxin. A model for this protein-protein interaction is proposed.
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Structure of cytochrome c nitrite reductase
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This enzyme is a key component of the nitrogen cycle and catalyses the reduction of nitrite to ammonia. The 3D structure was used to provide a reaction mechanism for the transformation of the nitrite. The structure also shows a close-packed arrangement of 10 c-type cytochromes, one of which is unusually coordinated to a lysine.
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0032731077
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Open conformation of a flavocytochrome c3 fumarate reductase
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The open conformation of fcc3 in this structure shows the domain movement required to allow the fumarate substrate to enter.
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This high resolution (1.8 Å) structure shows a malate-like intermediate trapped in the active site. Details of the mechanism are deduced from the structure which shows a probable proton pathway used to reduce the fumarate and the involvement of a conserved arginine side-chain acting as the proton donor for fumarate reduction.
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Structure of fumarate reductase from Wolinella succinogenes at 2.2 angstrom resolution
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This membrane-bound fumarate reductase shares a similar active site to that of the soluble fcc3 structures. The structure suggests an electron transfer pathway that carries electrons from the quinol-oxidising site in the membrane via two haem groups and three Fe-S clusters to the FAD at the active site.
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Lancaster C.R.D., Kroger A., Auer M., Michel H. Structure of fumarate reductase from Wolinella succinogenes at 2.2 angstrom resolution. Nature. 402:1999;377-385. This membrane-bound fumarate reductase shares a similar active site to that of the soluble fcc3 structures. The structure suggests an electron transfer pathway that carries electrons from the quinol-oxidising site in the membrane via two haem groups and three Fe-S clusters to the FAD at the active site.
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0033580880
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Structure of the Escherichia coli fumarate reductase respiratory complex
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Despite a resolution of only 3.3 Å, the structure of this integral membrane protein showed remarkable detail and many similarities with the soluble fcc3 structures. The electron transfer pathway is similar to that found in Wolinella succinogenes. Two quinone groups are located on opposite sides of the membrane-bound domain.
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Iversen T.M., Luna Chavez C., Cecchini G., Rees D.C. Structure of the Escherichia coli fumarate reductase respiratory complex. Science. 284:1999;1961-1966. Despite a resolution of only 3.3 Å, the structure of this integral membrane protein showed remarkable detail and many similarities with the soluble fcc3 structures. The electron transfer pathway is similar to that found in Wolinella succinogenes. Two quinone groups are located on opposite sides of the membrane-bound domain.
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Crucially, these structures show that pterin binding does not stabilise the dimer interface. In the presence of zinc, four cysteine residues form a zinc-tetrathiolate complex which stabilises the dimer. In the absence of zinc, two symmetry related cysteines form disulfide bonds.
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