Linked Life Data

6304055

Source:http://linkedlifedata.com/resource/pubmed/id/6304055

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1983-7-15
pubmed:abstractText
Acidification of a salt-free solution of native low spin globular horse heart ferricytochrome c with HCl causes a single cooperative transition centered at pH 2.5 at 23 degrees C resulting in the formation of denatured high spin ferricytochrome c. By contrast, acidification with HCIO4 uncouples denaturation from the spin-state transition, resulting in the formation of a globular high spin form of ferricytochrome c at pH 0.0 exhibiting only modest conformational differences from native cytochrome c as judged by far ultraviolet circular dichoroic, tryptophan fluorescence, and reduced viscosity measurements. This uncoupling is consistent with the preferential binding of two perchlorate anions to the globular form(s) cytochrome c. The acid spin-state transition of the perchlorate complex is biphasic, having midpoint values at pH 0.7 and 3.6 involving 1.0 and 1.6 protons, respectively, when measured in the presence of 1 M perchlorate.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
258
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
6772-6
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
A globular high spin form of ferricytochrome c.
pubmed:publicationType
Journal Article