Amide proton exchange rates of oxidized and reduced saccharomyces cerevisiae iso-1-cytochrome c
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چکیده
منابع مشابه
Conformational Toggling of Yeast Iso-1-Cytochrome c in the Oxidized and Reduced States
To convert cyt c into a peroxidase-like metalloenzyme, the P71H mutant was designed to introduce a distal histidine. Unexpectedly, its peroxidase activity was found even lower than that of the native, and that the axial ligation of heme iron was changed to His71/His18 in the oxidized state, while to Met80/His18 in the reduced state, characterized by UV-visible, circular dichroism, and resonance...
متن کاملA mutation allowing an mRNA secondary structure diminishes translation of Saccharomyces cerevisiae iso-1-cytochrome c.
The CYC1-239-O mutation in the yeast Saccharomyces cerevisiae produces a -His-Leu- replacement of the normal -Ala-Gly- sequence at amino acid positions 5 and 6, which lie within a dispensable region of iso-1-cytochrome c; this mutation can accommodate the formation of a hairpin structure at the corresponding site in the mRNA. The amount of the altered protein was diminished to 20% of the wild-t...
متن کاملIsolation and sequence of the gene for iso-2-cytochrome c in Saccharomyces cerevisiae.
The two apocytochrome c proteins of yeast are coded for by separate genes. Iso-2-cytochrome c differs from the iso-1 protein at 17 positions within a homologous sequence of 108 amino acids. The previously cloned iso-1-cytochrome c coding sequence has been used to identify lambda-yeast recombinant phage containing the gene for iso-2-cytochrome c. The latter protein contains the dipeptide Ala-Ala...
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A strategy has been developed to express and purify a recombinant, nonfunctional axial-ligand mutant of iso-1-cytochrome c (Met-80-->Ala) in Saccharomyces cerevisiae in quantities necessary for extensive biophysical characterization. It involves coexpressing in the same plasmid (YEp213) the nonfunctional gene with a functional gene copy for complementation in a selective medium. The functional ...
متن کاملStructural Characteristics of Stable Folding Intermediates of Yeast Iso-1-Cytochrome-c
Cytochrome-c (cyt-c) is an electron transport protein, and it is present throughout the evolution. More than 280 sequences have been reported in the protein sequence database (www.uniprot.org). Though sequentially diverse, cyt-c has essentially retained its tertiary structure or fold. Thus a vast data set of varied sequences with retention of similar structure and fun...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1993
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560021118