A novel diazonium-sulfhydryl reaction in the inactivation of yeast alcohol dehydrogenase by diazotized 3-aminopyridine adenine dinucleotide

Diazotized 3-aminopyridine adenine dinucleotide has been found to modify four sulfhydryl groups per molecule of enzyme during the complete inactivation of yeast alcohol dehydrogenase. The reaction of sulfhydryl groups was indicated by titration studies with 5,5'- dithiobis (2-nitrobenzoic acid) as well as isolation and quantification of the cysteinyl derivative released by acid hydrolysis of the modified enzyme. The cysteinyl derivative was identified as S-(3-pyridyl) cysteine. Authentic S-(3-pyridyl) cysteine was synthesized and structurally characterized for these studies. Diazonium-sulfhydryl reactions were demonstrated for a number of diazonium derivatives with cysteine, homocysteine, glutathione and mercaptoethanol at 0-4° and neutral pH. Second order rate constants were determined in reactions of these sulfhydryl compounds with diazotized l-methyl-3-aminopyridinium chloride, diazotized 3-aminopyridine adenine dinucleotide and diazotized 3-aminopyridine adenine dinucleotide phosphate. Chemical studies of the diazonium-sulfhydryl reaction of diazotized p-aminobenzoic acid with cysteine indicated the initial formation of a diazomercaptide which can then decompose to yield the thioether.

Name thesis:degree_name

Ph. D.

Level thesis:degree_level

doctoral

Discipline thesis:degree_discipline

Biochemistry and Nutrition

Department dc:contributor.department

Biochemistry and Nutrition

Grantor dc:publisher

Virginia Polytechnic Institute and State University

Year dc:date.issued

1974

Author dc:creator

• Chan, Jack Cham-Kit

Statement dc:rights

• In Copyright

Licence dc:rights.uri

• http://rightsstatements.org/vocab/InC/1.0/

Language dc:language.iso

en

Handle dc:identifier.uri

http://hdl.handle.net/10919/74199

OAI identifier oai:identifier

oai:vtechworks.lib.vt.edu:10919/74199