Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles

Andrade, Susana L. A.; Brondino, Carlos D.; Kamenskaya, Elvira O.; Levashov, Andrey V.; Moura, José J. G.

doi:10.1016/s0006-291x(03)01337-8

Cited by 17 publications

(11 citation statements)

References 21 publications

(26 reference statements)

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“…200 kDa), in which each monomer contains the molybdenum active site and two FeS centres. Furthermore, we have recently shown that each monomer is catalytically active [9].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus

Thapper¹,

Rivas²,

Brondino³

et al. 2006

Journal of Inorganic Biochemistry

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“…200 kDa), in which each monomer contains the molybdenum active site and two FeS centres. Furthermore, we have recently shown that each monomer is catalytically active [9].…”

Section: Introductionmentioning

confidence: 99%

Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus

Thapper¹,

Rivas²,

Brondino³

et al. 2006

Journal of Inorganic Biochemistry

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“…3.7 nm based on its molecular weight (150,000D) and the hydrodynamic radius of the AOT reverse micelle at ω 0 = 30 was ca. 4.9 nm [15]. The size-fit principle fitted well for AOT reverse micelle.…”

Section: Stabilities Of Yadh In Different Reverse Micellesmentioning

confidence: 66%

Activity and kinetics studies of yeast alcohol dehydrogenase in a reverse micelle formulated from functional surfactants

Yun

Huang²,

et al. 2009

Open Chemistry

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Yeast alcohol dehydrogenase (YADH) showed substantial decrease in its catalytic activity due to the strong electrostatic interaction between the head groups of sodium bis(2-ethylhexyl) sulfosuccinate (AOT) and YADH in AOT reverse micelles. However, the catalytic activity of YADH in a nonionic reverse micellar interface (GGDE/TX-100) obtained from a functional nonionic surfactant N-gluconyl glutamic acid didecyl ester (GGDE) and Triton X-100 (TX-100) was higher than that in AOT reverse micelle under the respective optimum conditions. A comparison of the kinetic parameters showed that the turnover number k cat in GGDE/TX-100 reverse micelle was 1.4 times as large as that in AOT reverse micelle, but the Michaelis constants in AOT reverse micelle for ethanol K . The stability of YADH in GGDE/TX-100 reverse micelle was also found to be better than that in AOT reverse micelle. They were mainly attributed to the absence of electric charge on the head groups of GGDE and TX-100 in the GGDE/TX-100 reverse micelle. Warsaw and Springer-Verlag Berlin Heidelberg. © Versita

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“…Each of the monomers, which are catalytically independent [32], is organized into two major domains called Mo and FeS domains. The Mo domain is the largest one and contains the active site, whereas the FeS domain contains two [2Fe-2S] centers called FeS 1 and FeS 2.…”

Section: Introductionmentioning

confidence: 99%

Isotropic exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from Desulfovibrio gigas on native and polyalcohol inhibited samples: an EPR and QM/MM study

et al. 2014

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Aldehyde oxidoreductase from Desulfovibrio gigas (DgAOR) is a homodimeric molybdenum-containing protein that catalyzes the hydroxylation of aldehydes to carboxylic acids and contains a Mo-pyranopterin active site and two FeS centers called FeS 1 and FeS 2. The electron transfer reaction inside DgAOR is proposed to be performed through a chemical pathway linking Mo and the two FeS clusters involving the pyranopterin ligand. EPR studies performed on reduced as-prepared DgAOR showed that this pathway is able to transmit very weak exchange interactions between Mo(V) and reduced FeS 1. Similar EPR studies but performed on DgAOR samples inhibited with glycerol and ethylene glycol showed that the value of the exchange coupling constant J increases ~2 times upon alcohol inhibition. Structural studies in these DgAOR samples have demonstrated that the Mo-FeS 1 bridging pathway does not show significant differences, confirming that the changes in J observed upon inhibition cannot be ascribed to structural changes associated neither with pyranopterin and FeS 1 nor with changes in the electronic structure of FeS 1, as its EPR properties remain unchanged. Theoretical calculations indicate that the changes in J detected by EPR are related to changes in the electronic structure of Mo(V) determined by the replacement of the OHx labile ligand for an alcohol molecule. Since the relationship between electron transfer rate and isotropic exchange interaction, the present results suggest that the intraenzyme electron transfer process mediated by the pyranopterin moiety is governed by a Mo ligand-based regulatory mechanism.

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Kinetic behavior of Desulfovibrio gigas aldehyde oxidoreductase encapsulated in reverse micelles

Cited by 17 publications

References 21 publications

Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus

Biochemical and spectroscopic characterization of an aldehyde oxidoreductase isolated from Desulfovibrio aminophilus

Activity and kinetics studies of yeast alcohol dehydrogenase in a reverse micelle formulated from functional surfactants

Isotropic exchange interaction between Mo and the proximal FeS center in the xanthine oxidase family member aldehyde oxidoreductase from Desulfovibrio gigas on native and polyalcohol inhibited samples: an EPR and QM/MM study

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