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2,6-dichlorophenolindophenol
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cytochrome
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each subunit of the tetramer is composed of two domains, one binding a heme and the other an FMN prosthetic group. The cytochrome domain consists of residues 1 to 99
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FAD
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
cytochrome c
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cytochrome c
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
ferricytochrome c
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flavocytochrome b2
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FMN
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FMN
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one FMN per subunit
FMN
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one FMN per subunit
FMN
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each subunit of the tetramer is composed of two domains, one binding a heme and the other an FMN prosthetic group. The flavin binding domain contains a parallel beta8alpha8 barrel structure and is composed of residues 100 to 486. The FMN moiety, which is located at the C-terminal end of the central beta-barrel, is mostly sequestered from solvent. It forms hydrogen bond interactions with main- and side-chain atoms from six of the eight beta-strands. The interaction of Lys349 with atoms N-1 and O-2 of the flavin ring is probably responsible for stabilization of the anionic form of the flavin semiquinone and hydroquinone and enhancing the reactivity of atom N-5 toward sulfite. The binding of pyruvate at the active site in subunit 2 is stabilized by interaction of its carboxylate group with the side-chain atoms of Arg376 and Tyr143. Residues His373 and Tyr254 interact with the keto-oxygen atom and are involved in catalysis. In contrast, four water molecules occupy the substrate-binding site in subunit 1 and Tyr143 forms a hydrogen bond to the ordered heme propionate group. Otherwise the two flavin-binding domains are identical within experimental error
FMN
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the C-terminal domain of the enzyme contains FMN
FMN
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flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons
FMN
each of the four subunits contains a flavin mononucleotide prosthetic group
FMN
each of the four subunits contains a flavin mononucleotide prosthetic group
heme
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heme
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one heme per subunit
heme
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one heme per subunit
heme
one heme per subunit
heme
the flavoenzyme possesses flavocytochrome b2 subunits, that each consists of an N-terminal cytochrome domain and a C-terminal flavodehydrogenase, FDH, domain
heme
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the N-terminal domain of the enzyme contains protohaem IX
heme
each enzyme subunit contains a cytochrome b5-like heme domain
heme
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flavohemoprotein, in the crystal structure, FMN and heme are face to face, and appear to be in a suitable orientation and at a suitable distance for exchanging electrons. But in one subunit out of two, the heme domain is disordered and invisible. The heme domains are mobile in solution
heme
each of the four subunits contains a beta-type heme
heme
each of the four subunits contains a beta-type heme
additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
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ferricyanide used as electron acceptor
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additional information
ferricyanide used as electron acceptor
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
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electron acceptors other than ferricytochrome c used
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additional information
electron acceptors other than ferricytochrome c used
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additional information
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2,6-dichloroindophenol, ferricyanide, methylene blue, 1,2-naphthoquinone and cytochrome c can serve as electron acceptors
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additional information
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2,6-dichlorophenolindophenol used as electron acceptor, 10-fold more sensitive than ferricyanide
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additional information
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NAD+ and NADP+ cannot substitute, 2,6-dichlorophenolindophenol, ferricyanide and cytochrome c but not oxygen can serve as electron acceptor, rate of reduction with cytochrome c much slower than with the other possible acceptors
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additional information
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binding studies and models of the complex between cytochrome c and Fcb2, E63 is involved in the interaction with cyt. c, overview. Cytochrome c mutants E63K/D72K and E63K/D72K show reduced activity, but neither the K296M nor the Y97F mutation show significantly alteration of the enzyme kinetics. Effect of mutations on heme and cytochrome binding, overview
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additional information
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the enzyme is active with potassium ferricyanide
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additional information
FMN and heme groups are localized in two different domains
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additional information
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the enzyme lacks a heme-binding domain and the cytochrome c-binding domain
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