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Volumn 97, Issue 22, 2000, Pages 11954-11959
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The complex ATP-Fe2+ serves as a specific affinity cleavage reagent in ATP-Mg2+ sites of Na,K-ATPase: Altered ligation of Fe2+ (Mg2+) ions accompanies the E1P→E2P conformational change
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Author keywords
Energy transduction mechanism
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Indexed keywords
ADENOSINE TRIPHOSPHATASE (CALCIUM);
ADENOSINE TRIPHOSPHATASE (POTASSIUM SODIUM);
ADENOSINE TRIPHOSPHATE DERIVATIVE;
ADENOSINE TRIPHOSPHATE IRON;
ADENOSINE TRIPHOSPHATE MAGNESIUM;
ASCORBIC ACID;
HYDROGEN PEROXIDE;
IRON;
MAGNESIUM;
UNCLASSIFIED DRUG;
WATER;
ARTICLE;
CHEMICAL BOND;
CONTROLLED STUDY;
CRYSTAL STRUCTURE;
ENERGY TRANSFER;
ENZYME CONFORMATION;
ENZYME SUBUNIT;
HYDROLYSIS;
NUCLEOTIDE SEQUENCE;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
PROTEIN PHOSPHORYLATION;
ADENOSINE TRIPHOSPHATE;
ANIMALS;
BINDING SITES;
FERROUS COMPOUNDS;
HYDROLYSIS;
MAGNESIUM;
NA(+)-K(+)-EXCHANGING ATPASE;
PROTEIN CONFORMATION;
SWINE;
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EID: 0034710937
PISSN: 00278424
EISSN: None
Source Type: Journal
DOI: 10.1073/pnas.220332897 Document Type: Article |
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Times cited : (65)
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References (37)
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