Interaction of cytochrome c L with methanol dehydrogenase from Methylophaga marina 42:

Heiber-Langer, Irmgard; Cléry, Cécile; Franks, J. A.; Masson, Patrick; Balny, Claude

doi:10.1007/bf00185118

Cited by 10 publications

(1 citation statement)

References 43 publications

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“…The spectral transition is fully reversible and at high pressure, MEOH-DH retains its activity. In fact, at 400 MPa the speed of decoloration of Wurster's blue is accelerated by a factor of 4.5, which confirms and extends the data obtained by Heiber-Langer et al (1992) in the 1 to 200 MPa range.…”

Section: '( I )N( Li )D< M >D'supporting

confidence: 78%

Fourth derivative UV-spectroscopy of proteins under high pressure II. Application to reversible structural changes

et al. 1996

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The structural basis and the thermodynamics of pressure induced reversible spectral transitions in the fourth derivative ultraviolet absorbance spectra of proteins were analysed as described in the preceding paper. Three proteins were studied: adrenodoxin (a small iron-sulphur protein that serves as an electron donor for cytochrome P450scc), ribonuclease A, and methanol dehydrogenase (a tetrameric protein). Fourth derivative spectroscopy is used to probe important mechanistic aspects of these proteins. For adrenodoxin, the results suggest that one or two phenylalanines interact with the iron-sulphur redox centre. High pressure denaturation of ribonuclease leads to a molten globule like structure that also occurs as an intermediate in the high temperature induced denaturation process. This state is characterised by the local dielectric constant in the vicinity of tyrosines. Methanol dehydrogenase was found to be very stable towards pressure. High pressure appears to strengthen the interaction between the two a-subunits possibly through the increased interaction of four tryptophans with other aromatic amino acids.

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Section: '( I )N( Li )D< M >D'supporting

confidence: 78%

Fourth derivative UV-spectroscopy of proteins under high pressure II. Application to reversible structural changes

et al. 1996

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Proteins under pressure

Groß¹,

Jaenicke²

1994

EJB Reviews 1994

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Oceans not only cover the major part of the earth's surface but also reach into depths exceeding the height of the Mt Everest. They are populated down to the deepest levels (∼11 800 m), which means that a significant proportion of the global biosphere is exposed to pressures of up to 120 MPa. Although this fact has been known for more than a century, the ecology of the ‘abyss” is still in its infancy. Only recently, barophilic adaptation, i.e. the requirement of elevated pressure for viability, has been firmly established. In non‐adapted organisms, increased pressure leads to morphological anomalies or growth inhibition, and ultimately to cell death. The detailed molecular mechanism of the underlying ‘metabolic dislocation' is unresolved. Effects of pressure as a variable in microbiology, biochemistry and biotechnology allow the structure/function relationship of proteins and protein conjugates to be analyzed. In this context, stabilization by cofactors or accessory proteins has been observed. High‐pressure equipment available today allows the comprehensive characterization of the behaviour of proteins under pressure. Single‐chain proteins undergo pressure‐induced denaturation in the 100‐MPa range, which, in the case of oligomeric proteins or protein assemblies, is preceded by dissociation at lower pressure. The effects may be ascribed to the positive reaction volumes connected with the formation of hydrophobic and ionic interactions. In addition, the possibility of conformational effects exerted by moderate, non‐denaturing pressures, and related to the intrinsic compressibility of proteins, is discussed. Crystallization may serve as a model reaction of protein self‐organization. Kinetic aspects of its pressure‐induced inhibition can be described by a model based on the Oosawa theory of molecular association. Barosensitivity is known to be correlated with the pressure‐induced inhibition of protein biosynthesis. Attempts to track down the ultimate cause in the dissociation of ribosomes have revealed remarkable stabilization of functional complexes under pseudo‐physiological conditions, with the post‐translational complex as the most pressure‐sensitive species. Apart from the key issue of barosensitivity and barophilic adaptation, high‐pressure biochemistry may provide means to develop new approaches to nonthermic industrial processes, especially in the field of food technology.

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Enzyme Kinetics: Stopped-Flow Under Extreme Conditions

Balny

2002

Biological Systems Under Extreme Conditions

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Interaction of cytochrome c L with methanol dehydrogenase from Methylophaga marina 42:

Cited by 10 publications

References 43 publications

Fourth derivative UV-spectroscopy of proteins under high pressure II. Application to reversible structural changes

Fourth derivative UV-spectroscopy of proteins under high pressure II. Application to reversible structural changes

Proteins under pressure

Enzyme Kinetics: Stopped-Flow Under Extreme Conditions

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