Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1988-8-19
pubmed:abstractText
The brown membrane domain of Halobacterium halobium is a developmental precursor of the purple membrane and it contains a b-type cytochrome in addition to bacterio-opsin. In this report we provide spectroscopic evidence that the majority of the cytochrome content is a halobacterial cytochrome o. This cytochrome has absorption spectral properties in the oxidized, reduced, and CO liganded states which are characteristic of cytochrome o. The CD spectra show a complex bilobed pattern in the Soret spectral region which reflects the similarity of the heme environment to those of other b-type cytochromes involved in electron transport. We have also demonstrated a positive cooperativity of CO binding which, combined with CD spectral results, suggests two interacting heme moieties per cytochrome o. Size exclusion HPLC of solubilized brown membrane preparations shows a heme b containing protein with an Mr 42,000-46,000. The cytochrome may be easily separated from bacterio-opsin using a hydroxyapatite elution method on Triton X-100 solubilized preparations. The relative ease with which brown membrane disks may be oriented in high optical quality films should make the brown membrane a valuable model system for future spectroscopic investigations of cytochrome o.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0003-9861
pubmed:author
pubmed:issnType
Print
pubmed:volume
264
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
74-81
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Spectral evidence for cytochrome o in the brown membrane of Halobacterium halobium.
pubmed:affiliation
Department of Microbiology, Ohio State University, Columbus 43210.
pubmed:publicationType
Journal Article