EurekaMag.com logo
+ Site Statistics
References:
53,869,633
Abstracts:
29,686,251
+ Search Articles
+ Subscribe to Site Feeds
EurekaMag Most Shared ContentMost Shared
EurekaMag PDF Full Text ContentPDF Full Text
+ PDF Full Text
Request PDF Full TextRequest PDF Full Text
+ Follow Us
Follow on FacebookFollow on Facebook
Follow on TwitterFollow on Twitter
Follow on LinkedInFollow on LinkedIn

+ Translate

Irreversible extrusion of the first loop facing the matrix of the bovine heart mitochondrial ADP/ATP carrier by labeling the Cys(56) residue with the SH-reagent methyl methanethiosulfonate



Irreversible extrusion of the first loop facing the matrix of the bovine heart mitochondrial ADP/ATP carrier by labeling the Cys(56) residue with the SH-reagent methyl methanethiosulfonate



Journal of Biochemistry 127(3): 443-449



The effect of the SH-reagent methyl methanethiosulfonate (MMTS) on the ADP/ATP carrier of bovine heart mitochondria was studied under various conditions. MMTS labeled predominately Cys(56) in the first loop facing the matrix (loop M1), and the labeling inhibited ADP transport via the carrier. The transport inhibition was found to be due to fixation of the carrier in the m-state conformation. MMTS labeling was suggested not to affect ADP binding to its major binding site. These features were the same as those of another commonly used SH-reagent, N-ethylmaleimide (NEM). Although the van der Waals volume of the non-hydrogen-bondable methylthio group of MMTS is much smaller than that of the ethylsuccinimide group of NEM, modification of Cys(56) inhibited the interconversion between the m- and c-state conformation. The mechanism by which MMTS inhibited the transport activity is discussed in terms of stabilization of conformation of the loop M1.

(PDF emailed within 0-6 h: $19.90)

Accession: 010885730

Download citation: RISBibTeXText

PMID: 10731716

DOI: 10.1093/oxfordjournals.jbchem.a022626



Related references

Irreversible extrusion of the first loop facing the matrix of the bovine heart mitochondrial ADP. Journal of biochemistry 127(3): 443-449, 2000

Fluctuation of the first loop facing the matrix of the mitochondrial ADP/ATP carrier deduced from intermolecular cross-linking of Cys56 residues by bifunctional dimaleimides. Biochemistry 38(3): 1050-1056, 1999

Roles of adjoining Asp and Cys residues of first matrix-facing loop in transport activity of yeast and bovine mitochondrial ADP/ATP carriers. Journal of Biochemistry 139(3): 575-582, 2006

Specific labeling of the bovine heart mitochondrial phosphate carrier with fluorescein 5-isothiocyanate: roles of Lys185 and putative adenine nucleotide recognition site in phosphate transport. Journal of Biological Chemistry 276(13): 9792-9799, 2001

Conformation-dependent swinging of the matrix loop m2 of the mitochondrial Saccharomyces cerevisiae ADP/ATP carrier. Biochemistry 44(49): 16310-16320, 2005

Close location of the first loop to the third loop of the mitochondrial ADP/ATP carrier deduced from cross-linking catalyzed by copper-o-phenanthroline of the solubilized carrier with Triton X-100. Journal of Biochemistry 131(3): 461-468, 2002

Expression of the bovine heart mitochondrial ADP/ATP carrier in yeast mitochondria: Significantly enhanced expression by replacement of the N-terminal region of the bovine carrier by the corresponding regions of the yeast carriers. Biochimica et Biophysica Acta 1409(3): 113-124, Jan 5, 1999

Affinity labeling of a lysine residue in the coenzyme binding site of pig heart mitochondrial malate dehydrogenase. Biochemistry 18(21): 4683-4690, 1979

Specific labeling of membrane bound beef heart mitochondrial adp atp carrier with a photolabeled iodine 125 concentrated acyl coenzyme a. FASEB Journal 2(5): ABSTRACT 4793, 1988

Difference between yeast and bovine mitochondrial ADP/ATP carriers in terms of conformational properties of the first matrix loop as deduced by use of copper-o-phenanthroline. Biological & Pharmaceutical Bulletin 30(5): 885-890, 2007

Location of the dicyclohexylcarbodiimide-reactive glutamate residue in the bovine heart mitochondrial porin. Journal of Biological Chemistry 268(17): 12977-12982, 1993