Laser‐activated carbene labels the same residues in the proteolipid subunit of the ATP synthase in energized and nonenergized chloroplasts and mitochondria
Open Access
- 23 June 1986
- journal article
- Published by Wiley in FEBS Letters
- Vol. 202 (1) , 23-26
- https://doi.org/10.1016/0014-5793(86)80641-x
Abstract
The membrane‐embedded proteolipid of the Fo part of the ATP synthase in mitochondria (su 9) and chloroplasts (CFoIII) was labeled with a carbene generated from the photoactivatable hydrophobic reagent [125I]‐TID by a single UV‐laser pulse. Amino acid sequence analysis of the isolated proteolipid revealed that the carbene modified distinct residues which apparently are accessible from the lipid phase. No differences were detected in the labeling pattern upon energization of the membrane. Labeling of mitochondrial proteolipid in the presence of oligomycin led to a reduced modification of several side chains which map directly a surface involved in oligomycin binding.Keywords
This publication has 15 references indexed in Scilit:
- The mechanism of ATP synthase: A reassessment of the functions of the b and a subunitsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1986
- The slow rise of the flash-light-induced alkalization by Photosystem II of the suspending medium of thylakoids is reversibly related to thylakoid stackingBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1986
- Amino acid substitutions in mitochondrial ATPase subunit 9 of saccharomyces cerevisiae leading to oligomycin or venturicidin resistanceFEBS Letters, 1986
- Fluorescent analogs of N,N'-dicyclohexylcarbodiimide as structural probes of the bovine mitochondrial proton channelBiochemistry, 1985
- Membrane protein topology: amino acid residues in a putative transmembrane .alpha.-helix of bacteriorhodopsin labeled with the hydrophobic carbene-generating reagent 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirineBiochemistry, 1985
- The rate of ATP synthesis by reconstituted CF0F1 liposomesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1985
- Molecular mechanics of protonmotive F0F1 ATPasesFEBS Letters, 1985
- Structure of the membrane-embedded F0 part of F1F0 ATP synthase from Escherichia coli as inferred from labeling with 3-(trifluoromethyl)-3-(m-[125I]iodophenyl)diazirineBiochemistry, 1984
- Amino acid sequence of the proteolipid subunit of the ATP synthase from spinach chloroplastsFEBS Letters, 1980
- Characterization of Neurospora crassa Mitochondria Prepared with a Grind‐MillEuropean Journal of Biochemistry, 1970