Linked Life Data

11051564

Source:http://linkedlifedata.com/resource/pubmed/id/11051564

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2001-1-22
pubmed:abstractText
Cytochrome P450nor (P450nor) is a heme enzyme isolated from the denitrifying fungus Fusarium oxysporum and catalyzes the NO reduction to N2O. Crystal structures of the wild type and two Ser286 mutants (Ser286-->Val, Ser286-->Thr) of P450nor have been determined for the ferric resting forms at a 1.7 A resolution at cryogenic temperature (100 K). We carried out three comparative analyses: (1) between the structures of P450nor at room temperature and cryogenic temperature, (2) between the structures of P450nor and four monooxygenase P450s, and (3) between the structures of the WT and the Ser286 mutant enzymes of P450nor. Comparison of the charge distribution on the protein surface suggests that proton and electron flow to the heme site is quite different in P450nor than in monooxygenase P450s. On the basis of the mutant structures, it was found that a special hydrogen-bonding network, Wat99-Ser286-Wat39-Asp393-solvent, acts as a proton delivery pathway in NO reduction by P450nor. In addition, the positively charged cluster located beneath the B'-helix is suggested as possible NADH binding site in P450nor, from which the direct two-electron transfer to the heme site allows to generate the characteristic intermediate in the NO reduction. These structural characteristics were not observed in structures of monooxygenase P450s, implying that these are factors determining the unique NO reduction activity of P450nor.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0162-0134
pubmed:author
pubmed:issnType
Print
pubmed:day
31
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
191-205
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11051564-Binding Sites, pubmed-meshheading:11051564-Crystallography, X-Ray, pubmed-meshheading:11051564-Cytochrome P-450 Enzyme System, pubmed-meshheading:11051564-Electrons, pubmed-meshheading:11051564-Fusarium, pubmed-meshheading:11051564-Heme, pubmed-meshheading:11051564-Hydrogen Bonding, pubmed-meshheading:11051564-Kinetics, pubmed-meshheading:11051564-Ligands, pubmed-meshheading:11051564-Models, Molecular, pubmed-meshheading:11051564-Mutation, pubmed-meshheading:11051564-Nitric Oxide, pubmed-meshheading:11051564-Oxidoreductases, pubmed-meshheading:11051564-Protein Conformation, pubmed-meshheading:11051564-Protein Structure, Secondary, pubmed-meshheading:11051564-Protons, pubmed-meshheading:11051564-Recombinant Proteins, pubmed-meshheading:11051564-Serine, pubmed-meshheading:11051564-Spectrophotometry, pubmed-meshheading:11051564-Temperature, pubmed-meshheading:11051564-Threonine, pubmed-meshheading:11051564-Valine, pubmed-meshheading:11051564-Water
pubmed:year
2000
pubmed:articleTitle
Crystal structures of cytochrome P450nor and its mutants (Ser286-->Val, Thr) in the ferric resting state at cryogenic temperature: a comparative analysis with monooxygenase cytochrome P450s.
pubmed:affiliation
The Faculty of Science, Gakushuin University, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't