Literature DB >> 10550213

Structural bioenergetics and energy transduction mechanisms.

D C Rees1, J B Howard.   

Abstract

Life depends on transduction processes that couple cellular metabolism to environmental energy sources such as light or reduced compounds. These primary energy sources must be efficiently converted into forms that can be utilized by cells for biosynthesis, motility, transport, regulation, and other metabolic functions. In recent years, there has been an explosive increase in the determination of structures for proteins mediating energy transduction processes. These developments provide the opportunity to evaluate the structural basis for the efficient coupling of two energetic processes, which defines the area of structural bioenergetics. Here, we present some general features of energy transduction processes, including arguments that effective coupling of two processes by a transduction protein occurs by way of conformational states that are common to the catalysis of each process. This is illustrated by examples from the nucleotide switch family of proteins, with emphasis on the nitrogenase system where ATP hydrolysis is coupled to an electron transfer reaction. Copyright 1999 Academic Press.

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Year:  1999        PMID: 10550213     DOI: 10.1006/jmbi.1999.3005

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  19 in total

1.  Cooperative kinetics of both Hsp104 ATPase domains and interdomain communication revealed by AAA sensor-1 mutants.

Authors:  Douglas A Hattendorf; Susan L Lindquist
Journal:  EMBO J       Date:  2002-01-15       Impact factor: 11.598

2.  Analysis of the AAA sensor-2 motif in the C-terminal ATPase domain of Hsp104 with a site-specific fluorescent probe of nucleotide binding.

Authors:  Douglas A Hattendorf; Susan L Lindquist
Journal:  Proc Natl Acad Sci U S A       Date:  2002-02-26       Impact factor: 11.205

3.  Analysis of functional motions in Brownian molecular machines with an efficient block normal mode approach: myosin-II and Ca2+ -ATPase.

Authors:  Guohui Li; Qiang Cui
Journal:  Biophys J       Date:  2004-02       Impact factor: 4.033

4.  Gut pH as a limiting factor for digestive proteolysis in cultured juveniles of the gilthead sea bream (Sparus aurata).

Authors:  Lorenzo Márquez; Rocío Robles; Gabriel A Morales; Francisco J Moyano
Journal:  Fish Physiol Biochem       Date:  2011-11-16       Impact factor: 2.794

5.  Electron transfer precedes ATP hydrolysis during nitrogenase catalysis.

Authors:  Simon Duval; Karamatullah Danyal; Sudipta Shaw; Anna K Lytle; Dennis R Dean; Brian M Hoffman; Edwin Antony; Lance C Seefeldt
Journal:  Proc Natl Acad Sci U S A       Date:  2013-09-23       Impact factor: 11.205

6.  Insights into membrane association of Klebsiella pneumoniae NifL under nitrogen-fixing conditions from mutational analysis.

Authors:  Maria Milenkov; Robert Thummer; Jens Glöer; Joachim Grötzinger; Sascha Jung; Ruth A Schmitz
Journal:  J Bacteriol       Date:  2010-11-05       Impact factor: 3.490

7.  Energy Transduction in Nitrogenase.

Authors:  Lance C Seefeldt; Brian M Hoffman; John W Peters; Simone Raugei; David N Beratan; Edwin Antony; Dennis R Dean
Journal:  Acc Chem Res       Date:  2018-08-10       Impact factor: 22.384

8.  A master switch couples Mg²⁺-assisted catalysis to domain motion in B. stearothermophilus tryptophanyl-tRNA Synthetase.

Authors:  Violetta Weinreb; Li Li; Charles W Carter
Journal:  Structure       Date:  2012-01-11       Impact factor: 5.006

9.  The catalytic transition state in ATP synthase.

Authors:  A E Senior; J Weber; S Nadanaciva
Journal:  J Bioenerg Biomembr       Date:  2000-10       Impact factor: 2.945

10.  Structural basis for VO(2+)-inhibition of nitrogenase activity: (B) pH-sensitive inner-sphere rearrangements in the 1H-environment of the metal coordination site of the nitrogenase Fe-protein identified by ENDOR spectroscopy.

Authors:  Jan Petersen; Claire J Mitchell; Karl Fisher; David J Lowe
Journal:  J Biol Inorg Chem       Date:  2008-05       Impact factor: 3.358

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