The Purification and Characterization of the o-type Cytochrome Oxidase from Methylophilus methylotrophus, and its Reconstitution into a 'Methanol Oxidase' Electron Transport Chain

Microbiology ◽  
1984 ◽  
Vol 130 (9) ◽  
pp. 2201-2212
Author(s):  
S. J. FROUD ◽  
C. ANTHONY
Keyword(s):  
Electron Transport ◽  
Cytochrome Oxidase ◽  
Electron Transport Chain ◽  
Purification And Characterization ◽  
Methylophilus Methylotrophus ◽  
Transport Chain ◽  
Methanol Oxidase

scholarly journals Functional characterization of mutants deficient in N-terminal phosphorylation of the CF1 subunit beta

2021 ◽  
Author(s):  
Ralph Bock ◽  
Deserah D Strand ◽  
Daniel Karcher ◽  
Stephanie Ruf ◽  
Anne Schadach ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Electron Transport ◽  
Atp Synthase ◽  
Electron Transport Chain ◽  
Atp Hydrolysis ◽  
Molecular Motor ◽  
Functional Characterization ◽  
Phosphorylation Sites ◽  
Transport Chain

Understanding the regulation of photosynthetic light harvesting and electron transfer is of great importance to efforts to improve the ability of the electron transport chain to supply downstream metabolism. The central regulator of the electron transport chain is the ATP synthase, the molecular motor that harnesses the chemiosmotic potential generated from proton coupled electron transport to synthesize ATP. The ATP synthase is regulated both thermodynamically and post-translationally, with proposed phosphorylation sites on multiple subunits. In this study we focused on two N-terminal serines on the catalytic subunit beta, previously proposed to be important for dark inactivation of the complex to avoid ATP hydrolysis at night. Here we show that there is no clear role for phosphorylation in the dark inactivation of ATP synthase. Instead, mutation of one of the two phosphorylated serine residues to aspartate strongly decreased ATP synthase abundance. We propose that the loss of N-terminal phosphorylation of ATP beta may be involved in proper ATP synthase accumulation during complex assembly.

Purification and characterization of azurin from the methylamine-utilizing obligate methylotroph Methylobacillus flagellatus KT

2012 ◽  
Vol 58 (4) ◽  
pp. 516-522 ◽  
Author(s):  
Tatiana Y. Dinarieva ◽  
Stanislav A. Trashin ◽  
Jörg Kahnt ◽  
Arkady A. Karyakin ◽  
Alexander I. Netrusov
Keyword(s):  
Electron Transport ◽  
Methylamine Dehydrogenase ◽  
Purification And Characterization ◽  
Hydrogen Electrode ◽  
Periplasmic Fraction ◽  
Obligate Methylotroph ◽  
Wave Voltammetry ◽  
Transport Chain ◽  
Sds Page

Methylamine dehydrogenase (MADH) and azurin were purified from the periplasmic fraction of the methylamine-grown obligate methylotroph Methylobacillus flagellatus KT. The molecular mass of the purified azurin was 16.3 kDa, as measured by SDS–PAGE, or 13 920 Da as determined by MALDI–TOF mass spectrometry. Azurin of M. flagellatus KT contained 1 copper atom per molecule and had an absorption maximum at 620 nm in the oxidized state. The redox potential of azurin measured at pH 7.0 by square-wave voltammetry was +275 mV versus normal hydrogen electrode. MADH reduced azurin in the presence of methylamine, indicating that this cupredoxin is likely to be the physiological electron acceptor for MADH in the electron transport chain of the methylotroph. A scheme of electron transport functioning in M. flagellatus KТ during methylamine oxidation is proposed.

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