Purification of molybdenum cofactor and its fluorescent oxidation products

Claassen, V.; Oltmann, L. F.; Riet, J. van 't; Brinkman, U.A.Th.; Stouthamer, A. H.

doi:10.1016/0014-5793(82)80236-6

Cited by 13 publications

(9 citation statements)

References 11 publications

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“…Treatments which quantitatively release the non-covalently bound FAD from CO dehydrogenase, such as precipitation with perchloric acid or heat, did not liberate the MoCo, indicating its comparatively tight integration into the enzyme [31]. In addition, FAD released from CO dehydrogenase remained intact and active, whereas MoCo released from protein linkage was extremely unstable in air and rapidly inactivated by unknown degradative pathways [12,[44][45][46][47][48][49]. This explains why MoCo does not exist stably in a free and soluble state unless special precautions are taken.…”

Section: Molybdenum Cofactormentioning

confidence: 99%

Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria

Meyer

Jacobitz

Krüger

1986

FEMS Microbiology Letters

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The use of CO as a growth substrate by aerobic CO‐oxidizing (carboxydotrophic) bacteria requires some features not obvious in other bacteria. These are the presence of the enzyme CO dehydrogenase, a branched respiratory chain with an alternative CO‐insensitive terminal oxidase (cytochrome b653) and formation of reduced pyridine nucleotides by a pmf‐driven reversed electron transfer. Immunocytochemical localization studies revealed that CO dehydrogenase is attached to the inner aspect of the cytoplasmic membrane of Pseudomonas carboxydovorans. The enzyme is a molybdo iron‐sulfur flavoprotein containing bactopterin as the organic portion of the molybdenum cofactor. Recent findings suggest that this novel pterin is universal to eubacterial molybdenum enzymes, whereas molybdopterin is universal to eukaryotic molybdoenzymes.

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Section: Molybdenum Cofactormentioning

confidence: 99%

Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria

Meyer

Jacobitz

Krüger

1986

FEMS Microbiology Letters

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“…On the other hand, the genes required for molybdenum cofactor production have been studied intensively. The cofactor is a pterin ring structure which is extremely oxygen labile (6,19). The production of the pterin cofactor, the addition of molybdenum to this molecule, and the insertion of the molybdopterin into apomolybdoenzymes require the products of eight genes in E. coli: chlA, B, D, E, F, G, M, and N (10,20,36,37).…”

mentioning

confidence: 99%

Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli

Pierson

Campbell

1990

J Bacteriol

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Clones of the Escherichia coli bisC locus have been isolated by complementing a bisC mutant for growth with d-biotin d-sulfoxide as a biotin source. The complementation properties of deletions and Tn5 insertions located the bisC gene to a 3.7-kilobase-pair (kbp) segment, 3.3 kbp of which has been sequenced. A single open reading frame of 2,178 bp, capable of encoding a polypeptide of molecular weight 80,905, was found. In vitro transcription of plasmids carrying the wild-type sequence and deletion and insertion mutants showed that BisC complementation correlated perfectly with production of a polypeptide whose measured molecular weight (79,000) does not differ significantly from 80,905.

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“…It seems here, with all four inhibitors tested, that the blue fluorescing component becomes slightly less fluorescent (i.e. more reduced if it is a pteridine; Johnson et al 1980, Claassen et al 1982. One would expect an increase in its fluorescence when the flavin was blocked if it acted as an effective antenna.…”

Section: Discussionmentioning

confidence: 81%

Fluorescence properties of plasma membranes from oats and cauliflower in relation to blue light physiology

Widell

Sundqvist²

1987

Physiologia Plantarum

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Fluorescence properties of plasma membranes from dark‐grown oat shoots (Avena saliva L. cv. Sol II) and from cauliflower inflorescences (Brassica oleracea L.) were investigated. Along with a flavin (with a possible connection to blue light physiology), a blue fluorescing component was present. The effect of NaN3, phenyl acetic acid (PAA), KI (flavin inhibitors) and salicylhydroxamic acid (SHAM; inhibitor of e.g. the blue light‐induced cytochrome b reduction) were followed with regard to the fluorescence properties of the two components as well as with regard to the light‐induced cytochrome b reduction (LIAC). A change in flavin fluorescence and LIAC occurred at about the same concentration of PAA and SHAM, while LIAC was much more sensitive to KI and NaN3 than was the fluorescence. Rapid freezing and thawing did not change the relative fluorescence emission from the flavin and blue fluorescing component, respectively, but storage at ‐20°C for one or two days increased the fluorescence, especially from the latter. There did not seem to be a tight coupling between the fluorescence properties of the blue fluorescing component (spectrally similar to a pteridine) and the flavin. Therefore, no conclusions could be drawn concerning their connection in blue light physiology, i.e. in processes such as phototropism.

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Purification of molybdenum cofactor and its fluorescent oxidation products

Cited by 13 publications

References 11 publications

Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria

Biochemistry and physiology of aerobic carbon monoxide-utilizing bacteria

Cloning and nucleotide sequence of bisC, the structural gene for biotin sulfoxide reductase in Escherichia coli

Fluorescence properties of plasma membranes from oats and cauliflower in relation to blue light physiology

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