FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2016004316> ?p ?o ?g. }

• W2016004316 endingPage "421" @default.
• W2016004316 startingPage "411" @default.
• W2016004316 abstract "The nitrogenase iron (Fe) protein binds two molecules of MgATP or MgADP, which results in protein conformational changes that are important for subsequent steps of the nitrogenase reaction mechanism. In the present work, isothermal titration calorimetry has been used to deconvolute the apparent binding constants (K'a1 and K'a2) and the thermodynamic terms (delta H' degree and delta S' degree) for each of the two binding events of MgATP or MgADP to either the reduced or oxidized states of the Fe protein from Azotobacter vinelandii. The Fe protein was found to bind two nucleotides with positive cooperativity and the oxidation state of the [4Fe-4S] cluster of the Fe protein was found to influence the affinity for binding nucleotides, with the oxidized ([4Fe-4S]2+) state having up to a 15-fold higher affinity for nucleotides when compared to the reduced ([4Fe-4S]1+) state. The first nucleotide binding reaction was found to be driven by a large favorable entropy change (delta S' degree = 10-21 cal mol-1 K-1), with a less favorable or unfavorable enthalpy change (delta H' degree = +1.5 to -3.3 kcal mol-1). In contrast, the second nucleotide binding reaction was found to be driven by a favorable change in enthalpy (delta H' degree = -3.1 to -13.0 kcal mol-1), with generally less favorable entropy changes. A plot of the associated enthalpy (-delta H' degree) and entropy terms (-T delta S' degree) for each nucleotide and protein binding reaction revealed a linear relationship with a slope of 1.12, consistent with strong enthalpy-entropy compensation. These results indicate that the binding of the first nucleotide to the nitrogenase Fe protein results in structural changes accompanied by the reorganization of bound water molecules, whereas the second nucleotide binding reaction appears to result in much smaller structural changes and is probably largely driven by bonding interactions. Evidence is presented that the total free energy change (delta G' degree) derived from the binding of two nucleotides to the Fe protein accounts for the total change in the midpoint potential of the [4Fe-4S] cluster." @default.
• W2016004316 created "2016-06-24" @default.
• W2016004316 creator A5034125673 @default.
• W2016004316 creator A5055436683 @default.
• W2016004316 creator A5080373573 @default.
• W2016004316 date "1999-01-01" @default.
• W2016004316 modified "2023-09-27" @default.
• W2016004316 title "Thermodynamics of nucleotide interactions with the Azotobacter vinelandii nitrogenase iron protein" @default.
• W2016004316 cites W1515548591 @default.
• W2016004316 cites W1545630838 @default.
• W2016004316 cites W1551787313 @default.
• W2016004316 cites W1586542060 @default.
• W2016004316 cites W1973316236 @default.
• W2016004316 cites W1977319410 @default.
• W2016004316 cites W1977759633 @default.
• W2016004316 cites W1983138565 @default.
• W2016004316 cites W1987907285 @default.
• W2016004316 cites W1998690723 @default.
• W2016004316 cites W1999018772 @default.
• W2016004316 cites W2000886713 @default.
• W2016004316 cites W2008838869 @default.
• W2016004316 cites W2010114421 @default.
• W2016004316 cites W2020357919 @default.
• W2016004316 cites W2022901826 @default.
• W2016004316 cites W2025509373 @default.
• W2016004316 cites W2033086287 @default.
• W2016004316 cites W2040412213 @default.
• W2016004316 cites W2040979973 @default.
• W2016004316 cites W2045768241 @default.
• W2016004316 cites W2049411484 @default.
• W2016004316 cites W2049690534 @default.
• W2016004316 cites W2057604487 @default.
• W2016004316 cites W2061407935 @default.
• W2016004316 cites W2069005428 @default.
• W2016004316 cites W2069712812 @default.
• W2016004316 cites W2078678839 @default.
• W2016004316 cites W2089851319 @default.
• W2016004316 cites W2095430926 @default.
• W2016004316 cites W2105767787 @default.
• W2016004316 cites W2122995056 @default.
• W2016004316 cites W2125771483 @default.
• W2016004316 cites W2163917615 @default.
• W2016004316 cites W2209820801 @default.
• W2016004316 cites W2224930125 @default.
• W2016004316 cites W2469901405 @default.
• W2016004316 cites W27082230 @default.
• W2016004316 cites W4244460320 @default.
• W2016004316 cites W947679176 @default.
• W2016004316 doi "https://doi.org/10.1016/s0167-4838(98)00251-9" @default.
• W2016004316 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/9989226" @default.
• W2016004316 hasPublicationYear "1999" @default.
• W2016004316 type Work @default.
• W2016004316 sameAs 2016004316 @default.
• W2016004316 citedByCount "22" @default.
• W2016004316 countsByYear W20160043162014 @default.
• W2016004316 countsByYear W20160043162016 @default.
• W2016004316 countsByYear W20160043162017 @default.
• W2016004316 countsByYear W20160043162018 @default.
• W2016004316 countsByYear W20160043162021 @default.
• W2016004316 crossrefType "journal-article" @default.
• W2016004316 hasAuthorship W2016004316A5034125673 @default.
• W2016004316 hasAuthorship W2016004316A5055436683 @default.
• W2016004316 hasAuthorship W2016004316A5080373573 @default.
• W2016004316 hasConcept C104317684 @default.
• W2016004316 hasConcept C107824862 @default.
• W2016004316 hasConcept C121332964 @default.
• W2016004316 hasConcept C141280058 @default.
• W2016004316 hasConcept C147789679 @default.
• W2016004316 hasConcept C156911925 @default.
• W2016004316 hasConcept C166014724 @default.
• W2016004316 hasConcept C178790620 @default.
• W2016004316 hasConcept C181440489 @default.
• W2016004316 hasConcept C185592680 @default.
• W2016004316 hasConcept C187250156 @default.
• W2016004316 hasConcept C202270520 @default.
• W2016004316 hasConcept C2776159390 @default.
• W2016004316 hasConcept C2776740245 @default.
• W2016004316 hasConcept C3288061 @default.
• W2016004316 hasConcept C512185932 @default.
• W2016004316 hasConcept C523546767 @default.
• W2016004316 hasConcept C537208039 @default.
• W2016004316 hasConcept C54355233 @default.
• W2016004316 hasConcept C55493867 @default.
• W2016004316 hasConcept C71240020 @default.
• W2016004316 hasConcept C8010536 @default.
• W2016004316 hasConcept C86803240 @default.
• W2016004316 hasConcept C97355855 @default.
• W2016004316 hasConceptScore W2016004316C104317684 @default.
• W2016004316 hasConceptScore W2016004316C107824862 @default.
• W2016004316 hasConceptScore W2016004316C121332964 @default.
• W2016004316 hasConceptScore W2016004316C141280058 @default.
• W2016004316 hasConceptScore W2016004316C147789679 @default.
• W2016004316 hasConceptScore W2016004316C156911925 @default.
• W2016004316 hasConceptScore W2016004316C166014724 @default.
• W2016004316 hasConceptScore W2016004316C178790620 @default.
• W2016004316 hasConceptScore W2016004316C181440489 @default.
• W2016004316 hasConceptScore W2016004316C185592680 @default.
• W2016004316 hasConceptScore W2016004316C187250156 @default.

• next