|
rdf:type |
|
|
lifeskim:mentions |
|
|
pubmed:issue |
4
|
|
pubmed:dateCreated |
1997-4-30
|
|
pubmed:abstractText |
The 2.8 A crystal structure of hydroxylamine oxidoreductase of a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea, is described. Twenty-four haems lie in the centre bottom of the trimeric molecule, localized in four clusters within each monomer. The haem clusters within the trimer are aligned to form a ring that has inlet and outlet sites. The inlet is occupied by a novel haem, P460, and there are two possible outlet sites per monomer formed by paired haems lying within a cavity or cleft on the protein surface. The structure suggests pathways by which electron transfer may occur through the precisely arranged haems and provides a framework for the interpretation of previous and future biochemical and genetic observations.
|
|
pubmed:commentsCorrections |
|
|
pubmed:language |
eng
|
|
pubmed:journal |
|
|
pubmed:citationSubset |
IM
|
|
pubmed:chemical |
|
|
pubmed:status |
MEDLINE
|
|
pubmed:month |
Apr
|
|
pubmed:issn |
1072-8368
|
|
pubmed:author |
|
|
pubmed:issnType |
Print
|
|
pubmed:volume |
4
|
|
pubmed:owner |
NLM
|
|
pubmed:authorsComplete |
Y
|
|
pubmed:pagination |
276-84
|
|
pubmed:dateRevised |
2006-11-15
|
|
pubmed:meshHeading |
pubmed-meshheading:9095195-Amino Acid Sequence,
pubmed-meshheading:9095195-Binding Sites,
pubmed-meshheading:9095195-Computer Simulation,
pubmed-meshheading:9095195-Crystallography, X-Ray,
pubmed-meshheading:9095195-Electron Transport,
pubmed-meshheading:9095195-Heme,
pubmed-meshheading:9095195-Hydroxylamine,
pubmed-meshheading:9095195-Hydroxylamines,
pubmed-meshheading:9095195-Models, Molecular,
pubmed-meshheading:9095195-Molecular Sequence Data,
pubmed-meshheading:9095195-Nitrosomonas,
pubmed-meshheading:9095195-Oxidoreductases,
pubmed-meshheading:9095195-Protein Conformation,
pubmed-meshheading:9095195-Software,
pubmed-meshheading:9095195-Surface Properties
|
|
pubmed:year |
1997
|
|
pubmed:articleTitle |
The 2.8 A structure of hydroxylamine oxidoreductase from a nitrifying chemoautotrophic bacterium, Nitrosomonas europaea.
|
|
pubmed:affiliation |
Department of Life Science, Faculty of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama, Japan.
|
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|
