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cytochrome
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state of cytochrome that is two equivalents of oxidation greater than the ferric form (Cpd I species), state of cytochrome that is one equivalent of oxidation greater than the ferric form (Cpd II species), two-electron-oxidized state of P450 or peroxidases containing both an oxoferryl center [FeIV=O] and either a tryptophanyl or tyrosyl radical, analogous to Cpd ES in cytochrome c peroxidase (Cpd ES species)
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cytochrome b5
a cytochrome P450 enzyme, cytochrome b5 is bound in the reduced CYP101-camphor-carbon monoxide complex, cytochrome b5 perturbs many of the same resonances in the complex as Pdx, including those for residues involved in substrate access to and orientation within the active site of CYP101, chemical shifts, overview
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FAD
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increase of activity, can replace FMN
additional information
catalytic turnover in P450cam requires the enzymes putidaredoxin (Pdx) and putidaredoxin reductase (Pdr), which mediate electron transfer from NADH to heme, the process is tightly coupled to substrate hydroxylation
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cytochrome m
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cytochrome m
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cytochrome P-450cam, essential, b-type heme-thiolate protein of P-450-class
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cytochrome m
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optimal ratio of putidaredoxin reductase, putidaredoxin, cytochrome m is 1:10:2
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cytochrome P450
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cytochrome P450
CYP101D2 is a cytochrome P450 monooxygenase
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cytochrome P450
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cytochrome P450cam
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cytochrome P450
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cytochrome P450cam, importance and role of the polar residues, e.g. Tyr33, involved in the Pdx-P450cam interaction, overview. Interaction key residues are Pdx Asp38, Arg66, and Trp106, as well as P450cam Arg109 and Arg112, crystal structure of the Pdx-P450cam complex
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cytochrome P450
the putidaredoxin reductase-camphor monooxygenase fusion enzyme shows the 450 nm Soret band characteristic of the CYP superfamily
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Ferredoxin
[2Fe-2S] ferredoxin
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Ferredoxin
the CYP101D2 likely ferredoxin-binding site on the proximal face is largely positively charged, similar to that of CYP101D1
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FMN
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FMN
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requirement, prosthetic group of putidaredoxin reductase
heme
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heme
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CYP101 is a heme monoxygenase
heme
heme-dependent monooxygenase
heme
structural, electronic, and catalytic properties of cytochrome P450cam are subtly altered when the cysteine that coordinates to the heme iron is replaced with a selenocysteine
NADH
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NADH
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requirement, reduces reductase flavoprotein and putidaredoxin, but not P450cam, in the absence of camphor
NADH
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is required for O2 activation
NADPH
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NADPH
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requirement, instead of NADH, with campholide as substrate, Pseudomonas sp. C5
putidaredoxin
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347695, 347697, 347698, 347699, 347700, 671535, 672760, 673037, 673071, 674152, 674438, 674474, 674959, 675234, 676280, 702301, 702820, 704713, 705331, 724338, 725602, 725873 -
putidaredoxin
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671612, 672083, 673054, 674197, 675233, 676941, 701533, 701902, 702698, 704181, 744343, 744365, 744704, 745613, 746282 -
putidaredoxin
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essential, iron-sulfur redox protein, Fe2S2*Cys4-class, e-transfer agent to and effector of cytochrome P450cam
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putidaredoxin
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cannot be replaced by other FeS-proteins or the phospholipid of the hepatic microsomal P450 system
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putidaredoxin
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the putidaredoxin-binding site is only minimally affected by cytochrome b5
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putidaredoxin
analysis of protein-protein interactions between enzyme and cofactor, structural changes upon complex formation, overview
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putidaredoxin
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binding causes conformational changes involving K+, in absence of K+ multiple conformations occur, overview
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putidaredoxin
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electron transfer from putidaredoxin to the ferric-superoxo enzyme form, overview
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putidaredoxin
the physiological reductant and effector
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putidaredoxin
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the reaction cycle requires two distinct electron transfer processes from the [2Fe-2S] containing putidaredoxin to P450cam, altered binding and electron transfer with the putidaredoxin mutant C73S, structure and model of oxidized and reduced forms, overview
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putidaredoxin
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the substrate-free oxyferrous enzyme also reacts readily with reduced putidaredoxin
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putidaredoxin
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wild-type and mutant C73S/C85S cofactor, the mutant shows about 2fold improved substrate conversion
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putidaredoxin
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binding of putidaredoxin converts a single X-proline amide bond in CYP101 from trans or distorted trans to cis
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putidaredoxin
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optimal ratio of putidaredoxin reductase, putidaredoxin, cytochrome m is 1:10:2
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putidaredoxin
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transferring electrons from NADH to P450cam in a coupled assay method
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putidaredoxin
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the physiological electron transfer partner protein contains a [2Fe-2S] cluster, energetic importance and role of the polar residues, e.g. Tyr33, involved in the Pdx-P450cam interaction, overview. Interaction key residues are Pdx Asp38, Arg66, and Trp106, as well as P450cam Arg109 and Arg112, crystal structure of the Pdx-P450cam complex
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putidaredoxin
cofactor putidaredxin-bound enzyme structure analysis using crystal structure, PDB ID 4JWS
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putidaredoxin
Pdx, the enzyme is highly specific for its reductase, with an absolute requirement for the native putidaredoxin (Pdx) to provide the second electron transfer, binding kinetics and thermodynamics with wild-type and mutant enzymes, overview. Upon binding ferric P450cam, Pdx is now known to trigger a conformational change in the enzyme, which may provide the trigger to coordinate enzyme turnover and protect the enzyme from oxidative damage
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putidaredoxin
the catalytic cycle of P450cam requires two electrons, both of which are donated by putidaredoxin (Pdx), a ferredoxin containing a [2Fe-2S] cluster, structures of the Pdx-P450cam complex, potential electron transfer pathways and interactions between Pdx Asp38 and P450cam Arg112, as well as hydrophobic contacts between the Pdx Trp106 and P450cam residues, favorable interactions exist between Pdx Tyr33 and P450cam Asp125, as well as between Pdx Ser42 and P450cam His352, overview
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putidaredoxin
[2Fe-2S] putidaredoxin, Pdx. Camphor-bound ferric P450cam domain forms a complex with Pdx, modeling
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