Evidence for voltage-sensitive reaction steps in the mechanism of the red beet plasma membrane H+-ATPase

Briskin, Donald P.; Gawienowski, Margaret

doi:10.1016/s0981-9428(98)80043-0

Plant Physiology and Biochemistry

1998

DOI: 10.1016/s0981-9428(98)80043-0

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Evidence for voltage-sensitive reaction steps in the mechanism of the red beet plasma membrane H+-ATPase

Donald P. Briskin¹,

Margaret Gawienowski²

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2000

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Abolishment of Proton Pumping and Accumulation in the E1P Conformational State of a Plant Plasma Membrane H+-ATPase by Substitution of a Conserved Aspartyl Residue in Transmembrane Segment 6

Buch-Pedersen¹,

Venema²,

Serrano³

et al. 2000

Journal of Biological Chemistry

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؉ -transport. Proton pumping by the reconstituted mutant enzyme was completely abolished, whereas ATP was still hydrolyzed. The mutant was insensitive to the inhibitor vanadate, which preferentially binds to P-type ATPases in the E 2 conformation. During catalysis the Asp 684 3 Asn enzyme accumulated a phosphorylated intermediate whose stability was sensitive to addition of ADP. We conclude that the mutant enzyme is locked in the E 1 conformation and is unable to proceed through the E 1 P-E 2 P transition. P-type ATPases are relatively small ion pumps with a single catalytic subunit, and are characterized by forming a phosphorylated (hence P-type) intermediate during the reaction cycle (1). Plant plasma membrane H ϩ -ATPases belong to the subgroup of P 3 -type ATPases, which comprises proton pumps and is closely related to the subgroup of P 2 -type ATPases, which includes cation pumps such as the mammalian Na ϩ /K ϩ -, Ca 2ϩ -, and H ϩ

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Abolishment of Proton Pumping and Accumulation in the E1P Conformational State of a Plant Plasma Membrane H+-ATPase by Substitution of a Conserved Aspartyl Residue in Transmembrane Segment 6

Buch-Pedersen¹,

Venema²,

Serrano³

et al. 2000

Journal of Biological Chemistry

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show abstract

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Evidence for voltage-sensitive reaction steps in the mechanism of the red beet plasma membrane H+-ATPase

Cited by 1 publication

References 33 publications

Abolishment of Proton Pumping and Accumulation in the E1P Conformational State of a Plant Plasma Membrane H+-ATPase by Substitution of a Conserved Aspartyl Residue in Transmembrane Segment 6

Abolishment of Proton Pumping and Accumulation in the E1P Conformational State of a Plant Plasma Membrane H+-ATPase by Substitution of a Conserved Aspartyl Residue in Transmembrane Segment 6

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