Proteins with covalently bound heme or linear tetrapyrrole (bile pigment) prosthetic groups are present universally in having organisms. These proteins function in electron transport, photochemistry, and many other roles. This research is directed at the determination of the structure, stereochemistry, and biosynthesis of protein-bound tetrapyrroles with specific focus on biliverdin-derived bilin prosthetic groups of the phycobiliproteins. Small peptides bearing tetrapyrrole prosthetic groups will be isolated in pure form and their structure and stereochemistry determined by a combination of techniques, including 1H NMR, fast atom bombardment mass spectrometry, circular dichroism, and, where possible, by comparison with reference compounds, either derived by degradation of tetrapyrrole-bearing proteins with known crystal structures, or by synthesis. A sensitive in vitro fluorescence assay has been developed for the measurement of the addition of linear tetrapyrroles to apophycobiliproteins and will be utilized for the detection of precursor compounds and enzymes involved in their synthesis and attachment to the polypeptides. Molecular genetic approaches to the identification of such enzymes have also been devised.

National Institute of Health (NIH)
National Institute of General Medical Sciences (NIGMS)
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Biochemistry Study Section (BIO)
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University of California Berkeley
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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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