The Essential Arginine Residue at Position 210 in the a Subunit of the Escherichia coli ATP Synthase Can Be Transferred to Position 252 with Partial Retention of Activity
Open Access
- 1 December 1995
- journal article
- Published by Elsevier
- Vol. 270 (49), 29407-29412
- https://doi.org/10.1074/jbc.270.49.29407
Abstract
No abstract availableKeywords
This publication has 25 references indexed in Scilit:
- Second-site revertants of an arginine-210 to lysine mutation in the a subunit of the F0F1-ATPase from Escherichia coli: implications for structure.Proceedings of the National Academy of Sciences, 1992
- Role of the carboxyl terminal region of H+-ATPase (F0F1a subunit from Escherichia coliArchives of Biochemistry and Biophysics, 1991
- The Proton-Translocating ATPase of Escherichia ColiAnnual Review of Biophysics, 1990
- Proton Translocation by the F1FOATPase of Escherichia coliPublished by Elsevier ,1989
- The proton pore of the F0F1-ATPase of Escherichia coli: Ser-206 is not required for proton translocationBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1988
- The proton pore in the Escherichia coli F0F1-ATPase: A requirement for arginine at position 210 of the a-subunitBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1987
- The mechanism of ATP synthase: A reassessment of the functions of the b and a subunitsBiochimica et Biophysica Acta (BBA) - Bioenergetics, 1986
- The UNC operon nucleotide sequence, regulation and structure of ATP-synthaseBiochimica et Biophysica Acta (BBA) - Reviews on Bioenergetics, 1984
- An Asp—Asn substitution in the proteolipid subnit of the ATP‐synthase from Escherichia coli leads to a non‐functional proton channelFEBS Letters, 1982
- The proteolipid of a mutant ATPase from Escherichia coli defective in H+‐conduction contains a glycine instead of the carbodiimide‐reactive aspartyl residueFEBS Letters, 1980