Presence of molybdenum cofactor in seeds of wheat and barley

Alikulov, Z.A; Schiemann, Joachim

doi:10.1016/0168-9452(85)90197-9

Cited by 4 publications

(10 citation statements)

References 9 publications

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“…Molybdenum cofactor bound to a protein fraction of about 65 kDa has been previously reported in wheat and barley seeds (Alikulov and Schiemann 1985), and in winter wheat seeds (Vunkova-Radeva et al 1988). In all the cases, Mo-co could be detected without heating, a finding which was explained by assuming a spontaneous release of Mo-co from these proteins (Alikulov and Schiemann 1985).…”

Section: Discussionmentioning

confidence: 63%

“…In all the cases, Mo-co could be detected without heating, a finding which was explained by assuming a spontaneous release of Mo-co from these proteins (Alikulov and Schiemann 1985).…”

Section: Discussionmentioning

confidence: 77%

“…Though heat inactivation of free Mo-co and CP-Mo-co was very similar, it is noteworthy that after gel chromatography of these V. faba seed extracts the content of free Mo-co was low or undetactable but that of Mo-co bound to CP was high. As mentioned above, Mo-co that is bound to proteins and can be detected without any release treatment has also been reported (Alikulov and Schiemann 1985;Vunkova-Radeva et al 1988). Moreover Mo-co associated with CP can be assayed without adding molybdate, so it could be speculated that this is the way to separate readily available Mo-co (bound to CP) and "empty" free Mo-co (without Mo).…”

Section: Discussionmentioning

confidence: 87%

“…They contain a similar molybdenum cofactor (Mo-co) which is involved in both the constitution of the catalytic center, and the structural organization of the enzyme (Rajagopalan 1989). The presence of Mo-co has been reported in caryopses of wheat and barley (Alikulov and Schiemann 1985;VunkovaRadeva et al 1988), and in seeds of pea (Shvetsov et al 1992). The fact that legumes can assimilate both nitrate and dinitrogen might explain the accumulation of molybdenum by legume seeds (L'vov et al 1987) which would also be expected to contain relatively high amounts of Mo-co.…”

Section: Introductionmentioning

confidence: 93%

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Different forms of molybdenum cofactor inVicia faba seeds: The presence of molybdenum cofactor carrier protein and its purification

Kalakoutskii

Fernandez

1997

Planta

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Abstract. There were significant differences in the contents of molybdenum cofactor (Mo-co), both in a lowmolecular-mass form (free Mo-co) and in a protein-bound form, in seeds of seven Vicia faba genotypes. Lowmolecular-mass Mo-co species present in the extracts were detected by their ability to reactivate, through a dialysis membrane, aponitrate reductase from the Neurospora crassa nit-1 mutant. In extracts of all genotypes tested, the amount of Mo-co capable of directly reactivating nitrate reductase of the N. crassa nit-1 mutant was always much higher than that of low-molecular-mass Moco. These data cannot be explained by considering, as traditionally, that Mo-co detected directly, i.e. without any previous treatment for its release from Mo-coproteins, corresponds to free low-molecular mass Mo-co. A protein which bound Mo-co was purified to electrophoretic homogeneity. This protein consisted of a single 70-kDa polypeptide chain and carried a Mo-co that could be efficiently released when in contact with aponitrate reductase.

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Section: Discussionmentioning

confidence: 63%

“…In all the cases, Mo-co could be detected without heating, a finding which was explained by assuming a spontaneous release of Mo-co from these proteins (Alikulov and Schiemann 1985).…”

Section: Discussionmentioning

confidence: 77%

Section: Discussionmentioning

confidence: 87%

Section: Introductionmentioning

confidence: 93%

See 2 more Smart Citations

Different forms of molybdenum cofactor inVicia faba seeds: The presence of molybdenum cofactor carrier protein and its purification

Kalakoutskii

Fernandez

1997

Planta

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“…Therefore, the heat treatment steps were reduced, and the temperature requirements were changed. According to Alikulov and Schiemann, anaerobic and aerobic incubation in the presence of glutathione gave comparable results [13] . Thus, the heat treatment for the isolation of MoCo from the cell-free extract was performed under aerobic conditions in a water bath at 80 °C for 3 min and cooled on ice.…”

Section: мосо Isolation From Fish Internal Organsmentioning

confidence: 87%

Method for assessing the content of molybdenum enzymes in the internal organs of fish

Satkanov,

Tazhibay,

Zhumabekova

et al. 2024

MethodsX

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Molybdoenzymes and molybdenum cofactor in plants

Mendel

Hänsch

2002

Journal of Experimental Botany

240

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The transition element molybdenum (Mo) is essential for (nearly) all organisms and occurs in more than 40 enzymes catalysing diverse redox reactions, however, only four of them have been found in plants. (1) Nitrate reductase catalyses the key step in inorganic nitrogen assimilation, (2) aldehyde oxidase(s) have been shown to catalyse the last step in the biosynthesis of the phytohormone abscisic acid, (3) xanthine dehydrogenase is involved in purine catabolism and stress reactions, and (4) sulphite oxidase is probably involved in detoxifying excess sulphite. Among Mo-enzymes, the alignment of amino acid sequences permits domains that are well conserved to be defined. With the exception of bacterial nitrogenase, Mo-enzymes share a similar pterin compound at their catalytic sites, the molybdenum cofactor. Mo itself seems to be biologically inactive unless it is complexed by the cofactor. This molybdenum cofactor combines with diverse apoproteins where it is responsible for the correct anchoring and positioning of the Mo-centre within the holo-enzyme so that the Mo-centre can interact with other components of the enzyme's electron transport chain. A model for the three-step biosynthesis of Moco involving the complex interaction of six proteins will be described. A putative Moco-storage protein distributing Moco to the apoproteins of Mo-enzymes will be discussed. After insertion, xanthine dehydrogenase and aldehyde oxidase, but not nitrate reductase and sulphite oxidase, require the addition of a terminal sulphur ligand to their Mo-site, which is catalysed by the sulphur transferase ABA3.

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Presence of molybdenum cofactor in seeds of wheat and barley

Cited by 4 publications

References 9 publications

Different forms of molybdenum cofactor inVicia faba seeds: The presence of molybdenum cofactor carrier protein and its purification

Different forms of molybdenum cofactor inVicia faba seeds: The presence of molybdenum cofactor carrier protein and its purification

Method for assessing the content of molybdenum enzymes in the internal organs of fish

Molybdoenzymes and molybdenum cofactor in plants

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