Bacterial adenosine 5'-triphosphate synthase (F1F0): purification and reconstitution of F0 complexes and biochemical and functional characterization of their subunits.
Abstract
Receive: RSS Feeds, eTOCs, free email alerts (when new articles cite this article), more» Inrmation about commercial reprint orders: http://mmbr.asm.org/site/misc/reprints.xhtml To subscribe to to another ASM Journal go to: http://journals.asm.org/site/subscriptions/ MICROBIOLOGICAL REVIEWS, Dec. 1987, p. 477-497 Vol. 51, No. 4 0146-0749/87/040477-21$02.00/0 Copyright C) 1987, American Society r Microbiology Bacterial Adenosine 5'-Triphosphate Synthase (F1): Purification and of Complexes and Biochemical and Functional Characterization of Their Subunits ERWIN SCHNEIDER AND KARLHEINZ ALTENDORF* Fachbereich BiologielChemie, Universitat Osnabruck, D4500 Osnabruck, Federal Republic of Germany INTRODUCTION ............................. ............................. ............................. ............................. CRITERIA R FUNCTIONAL Passive Proton Translocation ............................. Interaction with F1 BACTERIAL COMPLEXES Preparations from PS 3 and ............................ Subunit Downloaded from http://mmbr.asm.org/ on December 24, 2011 by deepdyve Composition .............................4 79 480 Stoichiometry ............................. ........................... primary and Secondary Structures ........................... Role of Specific Amino Acid Residues ............................................................. Dissociation and Reassembly ............................................................. Similarities and Dissimilarities ............................................................. COMPARISON WITH MITOCHONDRIAL AND CHLOROPLAST SYSTEMS ................................ 486 Preparations ............................................................. Subunit Composition ............................................................. ............................................................. Chemical Modification ............................................................. of the DCCD-Binding Protein (Proteolipid) .......................................................... 488 OPEN QUESTIONS, PERSPECTIVES, AND MODELS ............................................................. ACKNOWLEDGMENTS ................. LITERATURE CITED ................. INTRODUCTION HW-translocating adenosine 5'-triphosphate (ATP) synthases are multisubunit enzymes which have been und in the cytoplasmic membranes of a variety of bacteria as