Carboxyl groups and the proton pump of bacteriorhodopsin

Conference · Mon Aug 01 00:00:00 EDT 1983

OSTI ID:5505431

Herz, J M; Packer, L

Chemical modification and spin-labeled studies of purple membranes isolated from Halobacterium halobium have provided the first evidence for buried carboxyl residues within the hydrophobic, membrane-protein domains. Spin label data showed that modification of buried carboxyl residues resulted in loss of protein activity. A pH-sensitive, chromophoric reporter group demostrated that a carboxyl residue in a hydrophobic membrane environment interacts with the retinal chromophore of bacteriorhodopsin. These results appear consistent with the idea that carboxyl residues in hydrophobic environments may be a general feature required for activity of membrane proton pumps.

• Research Organization: Lawrence Berkeley Lab., CA (USA)
• DOE Contract Number: AC03-76SF00098
• OSTI ID: 5505431
• Report Number(s): LBL-16446; CONF-8309178-1; ON: DE84001329
• Resource Relation: Conference: Conference on transport of proteins, ions and electrons through mitochondrial membranes, University College Cork, Ireland, 27 Sep 1983; Other Information: Portions are illegible in microfiche products
• Country of Publication: United States
• Language: English

Related Subjects

59 BASIC BIOLOGICAL SCIENCES
HYDROGEN IONS
MEMBRANE TRANSPORT
PHOTOSYNTHETIC MEMBRANES
BIOLOGICAL FUNCTIONS
PROTEINS
CONFORMATIONAL CHANGES
DERIVATIZATION
ELECTRON SPIN RESONANCE
BACTERIA
OCTADECANOIC ACID
CARBOXYLIC ACIDS
CHARGED PARTICLES
CHEMICAL REACTIONS
FUNCTIONS
IONS
MAGNETIC RESONANCE
MEMBRANES
MICROORGANISMS
MONOCARBOXYLIC ACIDS
ORGANIC ACIDS
ORGANIC COMPOUNDS
RESONANCE
550200* - Biochemistry