Abstract

Proteins with covalently bound heme and tetrapyrrole (bile pigment) prosthetic groups are a class of brilliantly clored, intensely fluorescent compounds found in all organisms. They have important roles in electron transport, photochemical reactions, and metabolic processes. The objectives of this investigation are to establish the structure and absolute stereochemistry of each pigement-peptide moiety, to establish the detailed biosynthetic mechanism by which each pigment-protein combination is formed, and to develop synthetic methods so that these molecules and their analogues will be available for structure-activity studies.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM028994-08
Application #
3276413
Study Section
Biochemistry Study Section (BIO)
Project Start
1982-05-01
Project End
1992-04-30
Budget Start
1989-05-01
Budget End
1990-04-30
Support Year
8
Fiscal Year
1989
Total Cost
Indirect Cost

  Institution

Name
University of California Berkeley
Department
Type
Schools of Arts and Sciences
DUNS #
094878337
City
Berkeley
State
CA
Country
United States
Zip Code
94704

  Publications

Schluchter, W M; Glazer, A N (1997) Characterization of cyanobacterial biliverdin reductase. Conversion of biliverdin to bilirubin is important for normal phycobiliprotein biosynthesis. J Biol Chem 272:13562-9
Lao, K; Glazer, A N (1996) Ultraviolet-B photodestruction of a light-harvesting complex. Proc Natl Acad Sci U S A 93:5258-63
Jung, L J; Chan, C F; Glazer, A N (1995) Candidate genes for the phycoerythrocyanin alpha subunit lyase. Biochemical analysis of pecE and pecF interposon mutants. J Biol Chem 270:12877-84
Fairchild, C D; Glazer, A N (1994) Nonenzymatic bilin addition to the alpha subunit of an apophycoerythrin. J Biol Chem 269:28988-96
Fairchild, C D; Glazer, A N (1994) Oligomeric structure, enzyme kinetics, and substrate specificity of the phycocyanin alpha subunit phycocyanobilin lyase. J Biol Chem 269:8686-94
Wemmer, D E; Wedemayer, G J; Glazer, A N (1993) Phycobilins of cryptophycean algae. Novel linkage of dihydrobiliverdin in a phycoerythrin 555 and a phycocyanin 645. J Biol Chem 268:1658-69
de Lorimier, R; Wilbanks, S M; Glazer, A N (1993) Genes of the R-phycocyanin II locus of marine Synechococcus spp., and comparison of protein-chromophore interactions in phycocyanins differing in bilin composition. Plant Mol Biol 21:225-37
Wilbanks, S M; Glazer, A N (1993) Rod structure of a phycoerythrin II-containing phycobilisome. I. Organization and sequence of the gene cluster encoding the major phycobiliprotein rod components in the genome of marine Synechococcus sp. WH8020. J Biol Chem 268:1226-35
Wilbanks, S M; Glazer, A N (1993) Rod structure of a phycoerythrin II-containing phycobilisome. II. Complete sequence and bilin attachment site of a phycoerythrin gamma subunit. J Biol Chem 268:1236-41
Fairchild, C D; Zhao, J; Zhou, J et al. (1992) Phycocyanin alpha-subunit phycocyanobilin lyase. Proc Natl Acad Sci U S A 89:7017-21

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