Substrate and substrate analogue binding properties of Renilla luciferase

Journal Article · Mon Nov 28 23:00:00 EST 1977 · Biochemistry; (United States)

OSTI ID:6935079

Matthews, J C; Hori, K; Cormier, M J

Luciferase from the anthozoan coelenterate Remilla reniformis catalyzes the oxidative decarboxylation of luciferin consuming 1 mol of O/sub 2/ per mol of luciferin oxidized and producing 1 mol of CO/sub 2/, 1 mol of oxyluciferin, and light (lambda/sub B/, 480 nm) with a 5.5 percent quantum yield. In this work we have examined the binding characteristics of luciferin, luciferin analogues, and competitive inhibitors of the luciferin-luciferase reaction. The results show that luciferin binding and orientation in the single luciferin binding site of luciferase are highly specific for and dependent upon the three group substituents of the luciferin molecule while the imidazolone-pyrazine nucleus of luciferin is not directly involved in binding. Anaerobic luciferin binding promotes a rapid concentration-dependent aggregation of luciferase which results in irreversible inactivation of the enzyme. This aggregation phenomenon is not observed upon binding of oxyluciferin, luciferyl sulfate, or luciferin analogues in which the substituent at the 2 position of the imidazolone-pyrazine ring has been substantially altered.

• Research Organization: Univ. of Georgia, Athens
• OSTI ID: 6935079
• Journal Information: Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 16:24; ISSN BICHA
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ALBUMINS
ANIMALS
BINDING ENERGY
BIOCHEMICAL REACTION KINETICS
CATALYSIS
CHEMICAL BONDS
CNIDARIA
ENERGY
ENZYME INHIBITORS
ENZYMES
INVERTEBRATES
KINETICS
LUCIFERASE
LUCIFERIN
ORGANIC COMPOUNDS
OXIDASES
OXIDOREDUCTASES
PROTEINS
REACTION KINETICS
SUBSTRATES