Linked Life Data

8880927

Source:http://linkedlifedata.com/resource/pubmed/id/8880927

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1997-1-22
pubmed:abstractText
Electrostatic properties on the protein surface were examined on the basis of the crystal structure of NADH-cytochrome b5 reductase refined to a crystallographic R factor of 0.223 at 2.1 A resolution and of the other three flavin-dependent reductases. A structural comparison of NADH-cytochrome b5 reductase with the other flavin-dependent reductases, ferredoxin-NADP+ reductase, phthalate dioxygenase reductase, and nitrate reductase, showed that the alpha/beta structure is the common motif for binding pyridine nucleotide. Although the amino acid residues associated with pyridine nucleotide-binding are not conserved, the electrostatic properties and the location of the pyridine nucleotide-binding pockets of NADH-requiring reductases were similar to each other. The electrostatic potential of the surface near the flavin-protruding side (dimethylbenzene end of the flavin ring) of NADH-cytochrome b5 reductase was positive over a wide area while that of the surface near the heme-binding site of cytochrome b5 was negative. This implied that the flavin-protruding side of NADH-cytochrome b5 reductase is suitable for interacting with its electron-transfer partner, cytochrome b5. This positive potential area is conserved among four flavin-dependent reductases. A comparison of the electron-transfer partners of four flavin-dependent reductases showed that there are significant differences in the distribution of electrostatic potential between inter-molecular and inter-domain electron-transfer reactions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0887-3585
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
32-41
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:8880927-Binding Sites, pubmed-meshheading:8880927-Chemical Phenomena, pubmed-meshheading:8880927-Chemistry, pubmed-meshheading:8880927-Crystallography, X-Ray, pubmed-meshheading:8880927-Cytochrome Reductases, pubmed-meshheading:8880927-Cytochrome-B(5) Reductase, pubmed-meshheading:8880927-Cytochromes b5, pubmed-meshheading:8880927-Electron Transport, pubmed-meshheading:8880927-Ferredoxin-NADP Reductase, pubmed-meshheading:8880927-Flavins, pubmed-meshheading:8880927-Hydrogen Bonding, pubmed-meshheading:8880927-Models, Molecular, pubmed-meshheading:8880927-Nitrate Reductase, pubmed-meshheading:8880927-Nitrate Reductases, pubmed-meshheading:8880927-Nucleotides, pubmed-meshheading:8880927-Oxidoreductases, pubmed-meshheading:8880927-Protein Conformation, pubmed-meshheading:8880927-Protein Structure, Secondary
pubmed:year
1996
pubmed:articleTitle
Electrostatic properties deduced from refined structures of NADH-cytochrome b5 reductase and the other flavin-dependent reductases: pyridine nucleotide-binding and interaction with an electron-transfer partner.
pubmed:affiliation
Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't