Preparation and characterization of chromium(III) and cobalt(III) complexes of adenosine 5'-O-(1-thiodiphosphate)

Lin, Irene; Hsueh, Amy; Dunaway‐Mariano, Debra

doi:10.1021/ic00180a012

Cited by 6 publications

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“…CD spectra that are characterized by a positive Cotton effect at Xjj^ (Lin et al, 1984b). The chromatographic and optical properties of these screw sense isomers are consistent with a A configuration.4 Likewise, the CrraADP screw sense isomers having the longest retention time on HPLC show a negative Cotton effect at Xmax, and these are assigned the A configuration.…”

Section: Discussionmentioning

confidence: 97%

“…However, by comparison of the physical and biochemical properties of the screw sense isomers of CrinADP with those of the analogous Co(III) and Rh(III) complexes, configurational assignment can be made with a reasonable degree of accuracy. For example, the A screw sense isomers of Rh(H20)4ADP, Co(NH3)4ADP, Cr-(H20)4ADPaS, Cr(NH3)4ADPaS, and Co(NH3)4ADPaS all have shorter retention times on reverse-phase HPLC (Lin et al, 1984b) than do their A isomers. In addition, the A screw isomers of these complexes display CD spectra characterized by a positive Cotton effect at Xmax [ca.…”

Section: Discussionmentioning

confidence: 99%

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Structural and biochemical properties of bidentate tetraaquarhodium(III) complexes of inorganic pyrophosphate and adenosine 5'-diphosphate

Shorter¹,

Haromy²,

Scalzo-Brush³

et al. 1987

Biochemistry

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The structural and biochemical properties of the alpha,beta-bidentate tetraaquarhodium(III) complexes of inorganic pyrophosphate [Rh(H2O)4PP] and adenosine diphosphate [Rh(H2O)4ADP] are examined. These Rh(III) complexes are exchange-inert analogues of the corresponding physiologically important MgIIPP and MgIIADP complexes. The crystal structure of [Rh(H2O)4H2P2O7]+Cl- shows that the six-membered chelate ring adopts a twist-boat conformation with an unusually high puckering amplitude of 0.756 (3) A. The Rh coordination distances average 2.02 (1) A, while the bridge P-O bonds are virtually equal in length. All 10 protons of the complex participate in hydrogen bonding. There are two intramolecular hydrogen bonds between the phosphate oxygen atoms and the axially coordinated water molecules. The Rh(H2O)4PP complex was found to be a substrate for yeast inorganic pyrophosphatase, with Ki = 0.063 (7) mM and Vm = 500 (100) min-1. The two screw sense isomers of Rh(H2O)4ADP were prepared from (Rp)-[alpha-16O,18O]ADP and assigned configuration on the basis of the magnitude of their 31P NMR isotopic chemical shifts. The Rh(H2O)4ADP complex binds a number of kinases as tightly as MgADP. Arginine kinase and creatine kinase were shown to bind the delta Rh(H2O)4ADP isomer 7 and 45 times tighter, respectively, than the lambda isomer. The reactivity of Rh(H2O)4PP with pyrophosphatase is comparable to that of Cr(H2O)4PP, and the binding affinities of the Rh(H2O)4ADP screw sense isomers for kinases are also comparable to those observed for the corresponding Cr(H2O)4ADP screw sense isomers.

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Section: Discussionmentioning

confidence: 97%

Section: Discussionmentioning

confidence: 99%

Structural and biochemical properties of bidentate tetraaquarhodium(III) complexes of inorganic pyrophosphate and adenosine 5'-diphosphate

Shorter¹,

Haromy²,

Scalzo-Brush³

et al. 1987

Biochemistry

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“…One explanation is that a conserved cysteine residue at the ATP binding site of various ATPases [30] may be positioned suitably only when the ATP binding site is in a conformation which allows ATP [or CO(NH~)~ATP] to bind with a low affinity site (Ez), to allow the formation of a Co-S coordination to replace one of the Co-0 coordinations in CO(NH,)~ATP. Studies with adenosine 5'-0-(I-thiodiphosphate) (ADP[aS]) using Cr(II1) and Co(II1) showed that the sulfur-coordinated CO(NH,)~ADP[~S] complex was thermodynamically more stable than the oxygen-coordinated C O ( N H~)~A D P [~S ] complex [31], whereas the sulfur-coordinated Cr(II1) complex was not observed. The reasons for the preference of Co-S coordination over Co-0 coordination are not clear.…”

Section: Discussionmentioning

confidence: 99%

How do MgATP analogues differentially modify high‐affinity and low‐affinity ATP binding sites of Na⁺/K⁺ ‐ATPase?

Serpersu

Bunk

Schoner

1990

European Journal of Biochemistry

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The exchange-inert tetra-ammino-chromium complex of ATP [Cr(NH3)4ATP], unlike the analogous cobalt complex CO(NH,)~ATP, inactivated Na + /K + -ATPase slowly by interacting with the high-affinity ATP binding .site. The inactivation proceeded at 37°C with an inactivation rate constant of 1.34 x lo-, min-' and with a dissociation constant of 0.62 pM. To assess the potential role of the water ligands of metal in binding and inactivation, a kinetic analysis of the inactivation of Na +/K +-ATPase by Cr(NH,),ATP, and its H20-substituted derivatives Cr(NH3),(H20)ATP, Cr(NH3)2(H20)zATP and Cr(H20)4ATP was carried out. The substitution of the H 2 0 ligands with NH3 ligands increased the apparent binding affinity and decreased the inactivation rate constants of the enzyme by these complexes. Inactivation by Cr(H20),ATP was 29-fold faster than the inactivation by Cr(NH3)4ATP. These results suggested that substitution to Cr(II1) occurs during the inactivation of the enzyme. Additionally hydrogen bonding between water ligands of metal and the enzyme's active-site residues does not seem to play a significant role in the inactivation of Naf/K+-ATPase by Cr(II1)-ATP complexes.Inactivation of the enzyme by Rh(HzO),ATP occurred by binding of this analogue to the high-affinity ATP site with an apparent dissociation constant of 1.8 pM. The observed inactivation rate constant of 2.11 x min-' became higher when Na' or Mg2+ or both were present. The presence of K f however, increased the dissociation constant without altering the inactivation rate constant. High concentrations of Na' reactivated the Rh(HzO),ATP-inactivated enzyme.Co (

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ChemInform Abstract: PREPARATION AND CHARACTERIZATION OF CHROMIUM(III) AND COBALT(III) COMPLEXES OF ADENOSINE 5′‐O‐(1‐THIODIPHOSPHATE)

Lin¹,

Hsueh²,

Dunaway‐Mariano³

1984

Chemischer Informationsdienst

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Preparation and characterization of chromium(III) and cobalt(III) complexes of adenosine 5'-O-(1-thiodiphosphate)

Cited by 6 publications

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Structural and biochemical properties of bidentate tetraaquarhodium(III) complexes of inorganic pyrophosphate and adenosine 5'-diphosphate

Structural and biochemical properties of bidentate tetraaquarhodium(III) complexes of inorganic pyrophosphate and adenosine 5'-diphosphate

How do MgATP analogues differentially modify high‐affinity and low‐affinity ATP binding sites of Na⁺/K⁺ ‐ATPase?

ChemInform Abstract: PREPARATION AND CHARACTERIZATION OF CHROMIUM(III) AND COBALT(III) COMPLEXES OF ADENOSINE 5′‐O‐(1‐THIODIPHOSPHATE)

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Preparation and characterization of chromium(III) and cobalt(III) complexes of adenosine 5'-O-(1-thiodiphosphate)

Cited by 6 publications

References 0 publications

Structural and biochemical properties of bidentate tetraaquarhodium(III) complexes of inorganic pyrophosphate and adenosine 5'-diphosphate

Structural and biochemical properties of bidentate tetraaquarhodium(III) complexes of inorganic pyrophosphate and adenosine 5'-diphosphate

How do MgATP analogues differentially modify high‐affinity and low‐affinity ATP binding sites of Na+/K+ ‐ATPase?

ChemInform Abstract: PREPARATION AND CHARACTERIZATION OF CHROMIUM(III) AND COBALT(III) COMPLEXES OF ADENOSINE 5′‐O‐(1‐THIODIPHOSPHATE)

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How do MgATP analogues differentially modify high‐affinity and low‐affinity ATP binding sites of Na⁺/K⁺ ‐ATPase?