STRUCTURE OF PROTEIN-BOUND BILE PIGMENTS

蛋白质结合胆汁色素的结构

• 批准号: 2175355
• 负责人: ALEXANDER N GLAZER
• 金额: $ 26.29万
• 依托单位: UNIVERSITY OF CALIFORNIA BERKELEY
• 依托单位国家: 美国
• 财政年份: 1982
• 资助国家: 美国
• 起止时间: 1982-05-01 至 1996-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2175355
• 关键词: bacterial genetics; bile pigments; chemical group; circular dichroism; fluorescence spectrometry; heme; high performance liquid chromatography; mass spectrometry; mutant; nuclear magnetic resonance spectroscopy; peptide structure; photosynthetic bacteria; phycobilin; porphyrin biosynthesis; porphyrin structure; protein biosynthesis; protein purification; protein sequence; protein structure; recombinant DNA; stereochemistry; tetrapyrroles

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.

蛋白质与共价结合血红素或线性四吡咯（胆汁）