Literature DB >> 17418931

Transport viewed as a catalytic process.

Martin Klingenberg1.   

Abstract

Transport catalysis is analysed in terms of the "induced transition fit" (ITF) concept. The essentials of ITF are briefly elucidated, emphasizing the difference of substrate-protein interactions between enzymes and carriers exemplified by the paradigm ADP/ATP carrier (AAC). Two of the numerous applications of the ITF are discussed in more detail: unidirectional passive and active transport and the relation of substrate site type inhibitors to the carrier conformations. According to ITF in most cases of unidirectional transport intrinsic binding energies may be insufficient for transport catalysis and requires additional energy from ATP or electrochemical gradients. The impacts of external energy on the carrier cycle are examined for ABC transporters (mdr) and for cation-substrate co-transporters (LacY). The relations of inhibitors to the binding site of the carrier are discussed, given the paradigm examples of side specific inhibitors of the AAC. Results with the AAC suggest the induction of an abortive ground state by inhibitors, representing extreme side specific conformation of the binding center.

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Year:  2007        PMID: 17418931     DOI: 10.1016/j.biochi.2007.02.010

Source DB:  PubMed          Journal:  Biochimie        ISSN: 0300-9084            Impact factor:   4.079


  12 in total

Review 1.  Understanding transport by the major facilitator superfamily (MFS): structures pave the way.

Authors:  Esben M Quistgaard; Christian Löw; Fatma Guettou; Pär Nordlund
Journal:  Nat Rev Mol Cell Biol       Date:  2016-01-13       Impact factor: 94.444

2.  Mitochondrial dynamics in heart cells: very low amplitude high frequency fluctuations in adult cardiomyocytes and flow motion in non beating Hl-1 cells.

Authors:  Nathalie Beraud; Sophie Pelloux; Yves Usson; Andrey V Kuznetsov; Xavier Ronot; Yves Tourneur; Valdur Saks
Journal:  J Bioenerg Biomembr       Date:  2009-04-28       Impact factor: 2.945

3.  Molecular basis of substrate-induced permeation by an amino acid antiporter.

Authors:  Lukasz Kowalczyk; Mercè Ratera; Antonella Paladino; Paola Bartoccioni; Ekaitz Errasti-Murugarren; Eva Valencia; Guillem Portella; Susanna Bial; Antonio Zorzano; Ignacio Fita; Modesto Orozco; Xavier Carpena; José Luis Vázquez-Ibar; Manuel Palacín
Journal:  Proc Natl Acad Sci U S A       Date:  2011-02-22       Impact factor: 11.205

4.  Substrate binding in the mitochondrial ADP/ATP carrier is a step-wise process guiding the structural changes in the transport cycle.

Authors:  Vasiliki Mavridou; Martin S King; Sotiria Tavoulari; Jonathan J Ruprecht; Shane M Palmer; Edmund R S Kunji
Journal:  Nat Commun       Date:  2022-06-23       Impact factor: 17.694

Review 5.  General principles of secondary active transporter function.

Authors:  Oliver Beckstein; Fiona Naughton
Journal:  Biophys Rev (Melville)       Date:  2022-03-29

6.  Poly(ADP-ribose) catabolism triggers AMP-dependent mitochondrial energy failure.

Authors:  Laura Formentini; Antonio Macchiarulo; Giulia Cipriani; Emidio Camaioni; Elena Rapizzi; Roberto Pellicciari; Flavio Moroni; Alberto Chiarugi
Journal:  J Biol Chem       Date:  2009-05-01       Impact factor: 5.157

7.  Electrostatic funneling of substrate in mitochondrial inner membrane carriers.

Authors:  Yi Wang; Emad Tajkhorshid
Journal:  Proc Natl Acad Sci U S A       Date:  2008-07-08       Impact factor: 11.205

8.  Mapping the nucleotide binding site of uncoupling protein 1 using atomic force microscopy.

Authors:  Rong Zhu; Anne Rupprecht; Andreas Ebner; Thomas Haselgrübler; Hermann J Gruber; Peter Hinterdorfer; Elena E Pohl
Journal:  J Am Chem Soc       Date:  2013-02-26       Impact factor: 15.419

Review 9.  The mitochondrial ADP/ATP carrier: functional and structural studies in the route of elucidating pathophysiological aspects.

Authors:  Véronique Trézéguet; Ludovic Pélosi; Guy J M Lauquin; Gérard Brandolin
Journal:  J Bioenerg Biomembr       Date:  2008-11-01       Impact factor: 3.853

10.  Formation of a cytoplasmic salt bridge network in the matrix state is a fundamental step in the transport mechanism of the mitochondrial ADP/ATP carrier.

Authors:  Martin S King; Matthew Kerr; Paul G Crichton; Roger Springett; Edmund R S Kunji
Journal:  Biochim Biophys Acta       Date:  2015-10-24
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