Classic papers on the quantification of respiratory proton ejection

Ian C. West

doi:10.1042/bio03705047

Classic papers on the quantification of respiratory proton ejection

The Biochemist ◽

10.1042/bio03705047 ◽

2015 ◽

Vol 37 (5) ◽

pp. 47-50

Author(s):

Ian C. West

Keyword(s):

Mitochondrial Respiration ◽

Chemiosmotic Theory ◽

Chemiosmotic Hypothesis ◽

Biochemical Journal ◽

Definitive Statement ◽

Classic Papers ◽

Journal Papers

This article looks at two Biochemical Journal papers that are frequently cited as the definitive statement of the quantitative support for Mitchell's chemiosmotic hypothesis in relation to mitochondrial respiration. Both are rich in methodological detail; both contain elaborations of chemiosmotic and biophysical theory. With these two papers, chemiosmotic theory entered the mainstream of bioenergetic thought.

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Signalling: the remarkable dynasties

The Biochemist ◽

10.1042/bio02801033 ◽

2006 ◽

Vol 28 (1) ◽

pp. 33-36

Author(s):

Robin Irvine

Keyword(s):

Biochemical Journal ◽

Metabolism Enzymes ◽

Journal Papers

The list of Biochemical Journal papers selected by the Editorial Board1–12 for the ‘classic’ status in signalling (plus a couple of directly relevant classics from the metabolism/enzymes section that I have included) consists almost entirely of papers with inositol or inositide in the title. This reflects a truly remarkable relationship between inositides, UK scientists and the Biochemical Journal.

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Conway's Microdiffusion Analysis: Eighty years on and still counting!

The Biochemist ◽

10.1042/bio03601034 ◽

2014 ◽

Vol 36 (1) ◽

pp. 34-39

Author(s):

Bartholomew Masterson

Keyword(s):

Volumetric Error ◽

Gaseous Diffusion ◽

Micro Scale ◽

The Third ◽

Biochemical Journal ◽

New Development ◽

A New Technique ◽

The Impact ◽

Classic Papers

Two papers published by Edward Joseph Conway became Biochemical Journal Classics; both of these concerned the micro-determination of ammonia. Broadly, the 1933 paper with Alfred Byrne described a new technique of general use for the analysis of substances (or products made from them) on a micro-scale that involved simple gaseous diffusion; the 1942 paper with Ethna O'Malley presented enhancements of this new development. In addition, over the period 1939–1963 Conway recapped the content of the classic papers and other related papers in eight editions (five revisions) of his book, Microdiffusion Analysis and Volumetric Error; the book greatly increased the impact of the microdiffusion technique, launched by the Biochemical Journal classic papers. Our story, starting with the isolation of ammonia, extends roughly over three 80-year periods; the first one ending when quantitative analysis by gaseous diffusion was achieved, the second with Conway and Byrne's innovation, and the third from then to the present day.

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Classics of cholesterol biosynthesis

The Biochemist ◽

10.1042/bio03204030 ◽

2010 ◽

Vol 32 (4) ◽

pp. 30-32

Author(s):

James R. Hanson

Keyword(s):

Cholesterol Biosynthesis ◽

Biochemical Journal ◽

Classic Papers

Five classic papers by Cornforth and Popjak published in the Biochemical Journal between 1953 and 1958, together with a lecture published in 1966, are reviewed and their impact on the understanding of cholesterol biosynthesis is described.

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Reading the phosphorylation code: binding of the 14-3-3 protein to multivalent client phosphoproteins

Biochemical Journal ◽

10.1042/bcj20200084 ◽

2020 ◽

Vol 477 (7) ◽

pp. 1219-1225 ◽

Cited By ~ 4

Author(s):

Nikolai N. Sluchanko

Keyword(s):

Protein Function ◽

Intrinsically Disordered Protein ◽

Structural Basis ◽

Major Protein ◽

Post Translational Modifications ◽

Protein Protein Interaction ◽

Intrinsically Disordered ◽

Biochemical Journal ◽

Multiple Binding ◽

And Control

Many major protein–protein interaction networks are maintained by ‘hub’ proteins with multiple binding partners, where interactions are often facilitated by intrinsically disordered protein regions that undergo post-translational modifications, such as phosphorylation. Phosphorylation can directly affect protein function and control recognition by proteins that ‘read’ the phosphorylation code, re-wiring the interactome. The eukaryotic 14-3-3 proteins recognizing multiple phosphoproteins nicely exemplify these concepts. Although recent studies established the biochemical and structural basis for the interaction of the 14-3-3 dimers with several phosphorylated clients, understanding their assembly with partners phosphorylated at multiple sites represents a challenge. Suboptimal sequence context around the phosphorylated residue may reduce binding affinity, resulting in quantitative differences for distinct phosphorylation sites, making hierarchy and priority in their binding rather uncertain. Recently, Stevers et al. [Biochemical Journal (2017) 474: 1273–1287] undertook a remarkable attempt to untangle the mechanism of 14-3-3 dimer binding to leucine-rich repeat kinase 2 (LRRK2) that contains multiple candidate 14-3-3-binding sites and is mutated in Parkinson's disease. By using the protein-peptide binding approach, the authors systematically analyzed affinities for a set of LRRK2 phosphopeptides, alone or in combination, to a 14-3-3 protein and determined crystal structures for 14-3-3 complexes with selected phosphopeptides. This study addresses a long-standing question in the 14-3-3 biology, unearthing a range of important details that are relevant for understanding binding mechanisms of other polyvalent proteins.

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