Carboxyl groups and the proton pump of bacteriorhodopsin

Conference · Mon Aug 01 04:00:00 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
• Country of Publication: United States
• Language: English

Related Subjects

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