Stability and structure of binary and ternary metal ion complexes with biocytin, the sulfoxide and sulfone, N-acetyl-L-lysine, and L-alanine

Griesser, Rolf; Prijs, Bernard; Sigel, Helmut; Föry, Werner; Wright, Lemuel D.; McCormick, Donald B.

doi:10.1021/bi00819a001

Cited by 29 publications

(14 citation statements)

References 18 publications

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“…Not only have we shown the involvement of certain metal ions, e.g., Zn 2+ , for specific enzymes , McCormick 1962, Sander et al 1965, but the general liganding properties of several important functional groups (Griessen et al 1971) including amino acids (Griesser et al 1969, Sigel et al 1969a, Sigel et al 1969b, Sigel et al 1977, Walker et al 1972, nucleotides (Sigel et al 1967, Sigel and, and such vitamins as biotin (Griesser et al 1970, Griesser et al 1973, Sigel et al 1969c, Sigel et al 1978a and lipoate (Sigel et al 1978a, Sigel et al 1978b have been delineated for important cations of the Irving-Williams series. These latter studies extend our knowledge of the possible interactions within biological metal ion-containing systems.…”

Section: Metal Ions Coordination With Biochemicals-k Becker R Griementioning

confidence: 89%

A Trail of Research on Cofactors: An Odyssey with Friends

McCormick

2000

The Journal of Nutrition

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Over the span of 40 y and with the participation of over 60 students and postdoctoral colleagues, my laboratory has been able to elucidate numerous aspects of cofactor metabolism and function. Findings have been on the absorption, transport, utilization and excretion of vitamin B-6, riboflavin, biotin, lipoate and ascorbate. Specificity studies on those trace but essential enzymes that catalyze conversion of such vitamins as B-6 and riboflavin to their functional coenzymes led to our development of "biochemically specific absorbents" that prototypically exemplified what later was called "affinity chromatography." Characterization of the purified kinases for B-6 and riboflavin revealed preference for Zn2+ with the eucaryotic enzymes and delimited effects of inhibitors that relate to drug action. Flavin adenine dinucleotide synthetase, separable from flavokinase in mammals, prefers Mg2+. Specifics for binding and function of flavocoenzymes were delineated for several flavoproteins. The flavin mononucleotide-dependent oxidase that converts the 5'-phosphates of pyridoxine and of pyridoxamine to pyridoxal phosphate is a connection between riboflavin and B-6 that we characterized in mechanistic detail and found to be the primary control point for conversion of B-6 to its coenzyme. Sequencing and cloning of a side-chain oxidase for riboflavin was achieved. Isolation and identification of metabolites of biotin and of lipoic acid, first from bacteria obtained by enrichment culture and then from mammals, provided seminal information on catabolic pathways involved, as have our other studies with flavin catabolites isolated from milk and urine.

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Section: Metal Ions Coordination With Biochemicals-k Becker R Griementioning

confidence: 89%

A Trail of Research on Cofactors: An Odyssey with Friends

McCormick

2000

The Journal of Nutrition

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“…Also the preference for Zn 2+ was established for flavokinase (McCormick, 1962; and bacterial dihydro-orotase (Sander et al 1965). The metal ion liganding properties of several important functional groups (Griesser et al 1971) including amino acids (Griesser et al 1969;McCormick et al 1969McCormick et al , 1974Sigel et al 1969aSigel et al ,b, 1970Sigel et al , 1972Sigel et al , 1977Walker et al 1972), nucleotides (Sigel et al 1967;, and such vitamins as biotin (Sigel et al 1969c(Sigel et al , 1978aGriesser et al 1970Griesser et al , 1973 and lipoate (Sigel et al 1978a,b) have been delineated for important cations of the Irving-Williams series. These latter studies extend our knowledge of the possible interactions within biological metal ion-containing systems.…”

Section: Metal Ionsmentioning

confidence: 99%

Micronutrient cofactor research with extensions to applications

McCormick

2002

Nutr. Res. Rev.

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Following identification of essential micronutrients, there has been a continuum of research aimed at revealing their absorption, transport, utilization as cofactors, and excretion and secretion. Among those cases that have received our attention are vitamin B 6 , riboflavin, biotin, lipoate, ascorbate, and certain metal ions. Circulatory transport and cellular uptake of the water-soluble vitamins exhibit relative specificity and facilitated mechanisms at physiological concentrations. Isolation of enzymes and metabolites from micro-organisms and mammals has provided information on pathways involved in cofactor formation and metabolism. Kinases catalysing phosphorylation of B 6 and riboflavin have a preference for Zn 2+ in stereospecific chelates with adenosine triphosphate. The synthetase for flavin adenine dinucleotide prefers Mg 2+ . The flavin mononucleotidedependent oxidase that converts the 5Ј-phosphates of pyridoxine and of pyridoxamine to pyridoxal phosphate is a connection between B 6 and riboflavin and is a primary control point for conversion of B 6 to its coenzyme. Sequencing and cloning of a side-chain oxidase for riboflavin was achieved. Details on binding and function have been delineated for some cofactor systems, especially in several flavoproteins. There is both photochemical oxidation and oxidative catabolism of B 6 and riboflavin. Both biotin and lipoate undergo oxidation of their acid side chains with redox cleavage of the rings. Applications from our findings include the development of affinity absorbents, enhanced drug delivery, delineation of residues in biopolymer modification, pathogen photoinactivation in blood components, and input into human dietary recommendations. Ongoing and future research in the cofactor arena can be expected to add to this panoply. At the molecular level, the way in which the same cofactor can participate in diverse catalytic reactions resides in interactions with surrounding enzyme structures that must be determined case by case. At the level of human intake, more knowledge is desirable for making micronutrient recommendations based on biochemical indicators, especially for the span between infancy and adulthood.

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“…This can be done by plotting the stability constants against the acidity constants. For a series of structurally related ligands, a straight line should result 5 ' 30 ' 31 . In fact, a plot of the data in Table 1 results in a line (empty circles) as seen in Fig.…”

Section: Structure Of the Binary And Ternary Complexes Cul And Cu(bimentioning

confidence: 99%

“…15). All these data were calculated by using the results of Tables 1 or 2 22 ' 34 , the literature n ' 31 and one of the previous or following equations:…”

Section: Cu = [Cu(bipy)l]_ Pcu(bipy L [Cu] [Bipy] [L]mentioning

confidence: 99%

Ternary Complexes in Solution, XII. Models for Biological Mixed-Ligand Complexes: 2,2′-Bipyridyl-Cu²⁺-Oligoglycine Systems

Sigel

Griesser

Prijs

1972

Zeitschrift Für Naturforschung B

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The stability constants of the binary Cu 2+ complexes of glycine amide, diglycine, diglycine amide, triglycine, and tetraglycine were determined, as were those of the mixed-ligand Cu 2+ systems containing 2,2'-bipyridyl and one of the mentioned oligoglycines. The results evidence that all these complexes have the same structure and, therefore, the binding sites of the ligands have to be the terminal amino group and the oxygen of the neighbored amide group. The stability differences between the ternary and the binary complexes are in agreement with this interpretation. It is of interest to note that these ternary complexes are significantly more stable than expected on statistical reasons. With increasing pH, the amide groups in the binary complexes are successively deprotonated. Thus, with tetraglycine finally all three amide protons are displaced, and the amide nitrogens are bound to the square-planar coordination sphere of Cu 2+ . As in the Cu 2+ -2,2'-bipyridyl 1 : 1 complex, only two coordination positions are left for the binding of the oligoglycine, in the tenary complexes, only one amide group can be deprotonated. An increase in pH with deprotonation of other amide groups leads to a displacement of 2,2'-bipyridyl, i. e. the simple binary complexes result. No evidence could be observed for the coordination of a deprotonated amide group to an apical position of the coordination sphere of Cu 2+ . Additionally, while the displacement of the first amide proton in the several binary Cu 2+ oligoglycine complexes occurs over a large pH range (4 to 7), the deprotonation in all the mixed-ligand complexes takes place at pH approximately 8.In peptides, and probably also in proteins, the deprotonated amide group is one of the important binding sites for the coordination of Cu 2+ 2 . In fact, quite a number of Cu 2+ -peptide complexes, including those with oligoglycines 3-8 , were investigated, and it was shown that the amide proton is lost by the coordination of this metal ion to the amide nitrogen.The aim of the present study was to learn how the coordination tendency between oligoglycines and Cu 2+ is influenced, if two positions are occupied by another ligand in the coordination sphere of the metal ion. In this way, a situation which is analogous to conditions present in biological systems may be simulated. Additionally, it seems important to understand the mutual influence of two ligands bound to the same metal ion, as such mixed-ligand complexes can be considered as models for enzymemetal ion-substrate complexes 9-12 . For example, in galactose oxidase action, the role of Cu 2+ has been suggested to lie in the formation of a ternary complex with the substrates 13 .Recently, it was shown 14 that in the mixed-ligand 2,2'-bipyridyl-Cu 2+ -glycine amide complex, the Requests for reprints should be sent to Priv.-Doz. Dr. HELMUT SIGEL, Institute of Inorganic Chemistry, Spitalstrasse 51, University of Basel, CH-4000 Basel (Switzerland) .amide group may still be deprotonated in the physiological pH range. However, the un...

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Stability and structure of binary and ternary metal ion complexes with biocytin, the sulfoxide and sulfone, N-acetyl-L-lysine, and L-alanine

Cited by 29 publications

References 18 publications

A Trail of Research on Cofactors: An Odyssey with Friends

A Trail of Research on Cofactors: An Odyssey with Friends

Micronutrient cofactor research with extensions to applications

Ternary Complexes in Solution, XII. Models for Biological Mixed-Ligand Complexes: 2,2′-Bipyridyl-Cu²⁺-Oligoglycine Systems

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Stability and structure of binary and ternary metal ion complexes with biocytin, the sulfoxide and sulfone, N-acetyl-L-lysine, and L-alanine

Cited by 29 publications

References 18 publications

A Trail of Research on Cofactors: An Odyssey with Friends

A Trail of Research on Cofactors: An Odyssey with Friends

Micronutrient cofactor research with extensions to applications

Ternary Complexes in Solution, XII. Models for Biological Mixed-Ligand Complexes: 2,2′-Bipyridyl-Cu2+-Oligoglycine Systems

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Ternary Complexes in Solution, XII. Models for Biological Mixed-Ligand Complexes: 2,2′-Bipyridyl-Cu²⁺-Oligoglycine Systems