N-Ethylmaleimide inhibition of the catalytic activities of the Dunaliella salina coupling factor 1 (CF1) and the restoration of the inhibition of the CF1 ATPase activity by N-ethylmaleimide

Selman-Reimer, Susanne; Duhé, Roy J.; Selman, Bruce R.

doi:10.1016/0005-2728(85)90217-8

Cited by 3 publications

(3 citation statements)

References 25 publications

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“…According to the reported observations the oxidized form of ovothiol A inhibits the light activated ATPase activity of the chloroplast coupling factor CF1. 25…”

Section: Biochemical Properties and Biological Functions Of Ovothiolmentioning

confidence: 99%

On ovothiol biosynthesis and biological roles: from life in the ocean to therapeutic potential

Castellano

Seebeck

2018

Nat. Prod. Rep.

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Covering: up to 2018Ovothiols are sulfur-containing natural products biosynthesized by marine invertebrates, microalgae, and bacteria. These compounds are characterized by unique chemical properties suggestive of numerous cellular functions. For example, ovothiols may be cytoprotectants against oxidative stress, serve as building blocks of more complex structures and may act as molecular messengers for inter- and intracellular signaling. Detailed understanding of ovothiol physiological role in marine organisms may unearth novel concepts in cellular redox biochemistry and highlight the therapeutic potential of this antioxidant. The recent discovery of ovothiol biosynthetic genes has paved the way for a systematic investigation of ovothiol-modulated cellular processes. In this highlight we review the early research on ovothiol and we discuss key questions that may now be addressed using genome-based approaches. This highlight article provides an overview of recent progress towards elucidating the biosynthesis, function and potential application of ovothiols.

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“…According to the reported observations the oxidized form of ovothiol A inhibits the light activated ATPase activity of the chloroplast coupling factor CF1. 25…”

Section: Biochemical Properties and Biological Functions Of Ovothiolmentioning

confidence: 99%

On ovothiol biosynthesis and biological roles: from life in the ocean to therapeutic potential

Castellano

Seebeck

2018

Nat. Prod. Rep.

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“…The second free sulfhydryl (S3) is not readily accessible, but becomes available when the thylakoid membrane is energized. Modification of S3 with maleimides inhibits both ATP synthesis and hydrolysis without affecting proton leakiness (10, 12 (6,20). When S3 (Cys-89) and S4 (Cys-322) of spinach y are…”

mentioning

confidence: 99%

“…With spinach thylakoids inhibition of CF, catalytic activities by monofunctional maleimides is energy dependent (10). Whereas with Dunaliella and Spirulina membranes maleimide inhibition of CF, does not require a light-induced protonmotive force (6,20). When S3 (Cys-89) and S4 (Cys-322) of cross-linked by bifunctional maleimides or by reagents that oxidize vicinal dithiols, e.g., DTNP, the thylakoids are rendered proton leaky (16).…”

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confidence: 99%

Sulfhydryl Reagents and Energy-Linked Reactions in Monocot Thylakoids

Cohen

Baxter²

1990

Plant Physiol.

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Monofunctional maleimides have been used to covalently modify the coupling factor protein of monocot thylakoid membranes. As with dicot thylakoids, incubation of the monocot thylakoids with maleimides in the light but not in the dark results in inhibition of both ATP synthesis and hydrolysis. In the dark, sites on the Y and subunits of maize Zea mays coupling factor 1 are modified after incubation of maize mesophyll thylakoids with the fluorescent maleimide N-(anilinonaphthyl-4) maleimide. A light accessible site localized solely to the y subunit has also been demonstrated. itaria sanguinalis]) with bifunctional maleimides or thiol oxidants in the light does not result in functional uncoupling, i.e the bifunctional reagents act more like energy transfer inhibitors. The lack of functional uncoupling could be due either to a failure of the reagents to cross-link key sulfhydryl residues in the y subunit or to the continued ability of the y subunit to gate proton movements through the chloroplast coupling factor complex even though its conformation has been altered by sulfhydryl reagents.The y subunit of the spinach proton-ATPase contains one disulfide bridge and two free sulfhydryls (9). One of the free sulffiydryls (S4 in McCarty's terminology [15]) is readily accessible to modification by maleimides in the dark. Modification of S4 has no apparent effect on energy transduction mediated by the coupling factor (CF,3). The second free sulfhydryl (S3) is not readily accessible, but becomes available when the thylakoid membrane is energized. Modification of S3 with maleimides inhibits both ATP synthesis and hydrolysis without affecting proton leakiness (10, 12 (6,20). When S3 (Cys-89) and S4 (Cys-322) of spinach y are

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Proton-Translocating ATPases

Al‐Awqati¹

1986

Annual Review of Cell and Developmental Biology

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N-Ethylmaleimide inhibition of the catalytic activities of the Dunaliella salina coupling factor 1 (CF1) and the restoration of the inhibition of the CF1 ATPase activity by N-ethylmaleimide

Cited by 3 publications

References 25 publications

On ovothiol biosynthesis and biological roles: from life in the ocean to therapeutic potential

On ovothiol biosynthesis and biological roles: from life in the ocean to therapeutic potential

Sulfhydryl Reagents and Energy-Linked Reactions in Monocot Thylakoids

Proton-Translocating ATPases

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