Literature DB >> 921767

Carbon-2 proton exchange at histidine-41 in bovine erythrocyte superoxide dismutase.

A E Cass, A O Hill, B E Smith.   

Abstract

The C-2 proton of one histidine residue in bovine erythrocyte superoxide dismutase is shown to be particularly labile. This residue is identified by tritiation, protein digestion and subsequent peptide 'mapping' as histidine-41. A half-life for the exchange of histidine C-2 1H for 2H in 2H2O as solvent, at pD 8.1 and 40 degrees C, is estimated as approx. 9.2h, by 1H nuclear-magnetic-resonance spectroscopy.

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Year:  1977        PMID： 921767      PMCID： PMC1164943          DOI： 10.1042/bj1650587

Source DB:  PubMed          Journal:  Biochem J        ISSN： 0264-6021            Impact factor:   3.857


  6 in total

1.  Correlation proton magnetic resonance studies at 250 MHz of bovine pancreatic ribonuclease. I. Reinvestigation of the histidine peak assignments.

Authors:  J L Markley
Journal:  Biochemistry       Date:  1975-08-12       Impact factor: 3.162

2.  pH dependence of tritium exchange with the C-2 protons of the histidines in bovine trypsin.

Authors:  M Krieger; R E Koeppe; R M Stroud
Journal:  Biochemistry       Date:  1976-08-10       Impact factor: 3.162

3.  Determination of pKa's of individual histidine residues in pancreatic ribonuclease by hydrogen-tritium exchange.

Authors:  M Oe; H Matsuo; F Sakiyama; K Narita
Journal:  J Biochem       Date:  1974-05       Impact factor: 3.387

4.  Bovine erythrocyte superoxide dismutase. Complete amino acid sequence.

Authors:  H M Steinman; V R Naik; J L Abernethy; R L Hill
Journal:  J Biol Chem       Date:  1974-11-25       Impact factor: 5.157

5.  Bovine erythrocyte cupro-zinc protein. 1. Isolation and general characterization.

Authors:  J Bannister; W Bannister; E Wood
Journal:  Eur J Biochem       Date:  1971-01

6.  Crystal structure of bovine Cu,Zn superoxide dismutase at 3 A resolution: chain tracing and metal ligands.

Authors:  J Richardson; K A Thomas; B H Rubin; D C Richardson
Journal:  Proc Natl Acad Sci U S A       Date:  1975-04       Impact factor: 11.205
  6 in total
  5 in total

1.  Zinc(II) binding to apo-(bovine erythrocyte superoxide dismutase).

Authors:  A E Cass; H A Hill; J V Bannister; W H Bannister
Journal:  Biochem J       Date:  1979-02-01       Impact factor: 3.857

2.  The exchange of histidine C-2 protons in superoxide dismutases. A novel method for assigning histidine-metal ligands in proteins.

Authors:  A E Cass; H A Hill; J V Bannister; W H Bannister; V Hasemann; J T Johansen
Journal:  Biochem J       Date:  1979-10-01       Impact factor: 3.857

3.  Investigation of human erythrocyte superoxide dismutase by 1H nuclear-magnetic-resonance spectroscopy.

Authors:  H A Hill; W K Lee; J V Bannister; W H Bannister
Journal:  Biochem J       Date:  1980-01-01       Impact factor: 3.857

4.  1H NMR investigation of reduced copper-cobalt superoxide dismutase.

Authors:  I Bertini; C Luchinat; M Piccioli; M V Oliver; M S Viezzoli
Journal:  Eur Biophys J       Date:  1991       Impact factor: 1.733

5.  A spectroscopic characterization of a monomeric analog of copper, zinc superoxide dismutase.

Authors:  I Bertini; M Piccioli; M S Viezzoli; C Y Chiu; G T Mullenbach
Journal:  Eur Biophys J       Date:  1994       Impact factor: 1.733
  5 in total

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