<sup>113</sup>Cd nuclear magnetic resonance of metallothionein

Sadler, Peter J.; Bakka, Arne; Beynon, P.

doi:10.1016/0014-5793(78)80965-x

Cited by 39 publications

(14 citation statements)

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“…43 and 44), features indicative of asymmetric coordination (Ulmer et al, 1962;Pulido et aI., 1966;Rupp and Weser, 1978;Buhler and Kagi, 1979;Vasak et al, 1981a,b). Recently, 'H-NMR and Il3Cd-NMR spectroscopy also showed that the cysteinyl residues of metallothionein participate in metal binding (Galdes et al, 1978;Sadler et al, 1978;Armitage, 1979, 1980a;Vasak et al, 1980). In addition, these studies indicate that other residues do not bind metal atoms (Vasak et al, 1980).…”

Section: The Metallobiochemistry Of Zinc Enzymes 403mentioning

confidence: 93%

“…This study also suggests that two distinct metal binding sites are present in metallothionein. Semiempirical analysis of the chargetransfer spectra for zinc, cadmium, and mercury metallothioneins confirms tetracoordination of each metal atom to four cysteinyl ligands (Vasak et al, 1981b), as do the II3Cd-NMR spectra of the 113Cd-substituted protein (Sadler et al, 1978;Otvos and Armitage, 1979). The 1'3Cd(II)-113Cd(II) coupling observed in these spectra Armitage, 1979, 1980a) demonstrates the presence of Satoms bridging the metals.…”

Section: The Metallobiochemistry Of Zinc Enzymes 403mentioning

confidence: 95%

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The Metallobiochemistry of Zinc Enzymes

Vallée

Galdes

1984

Advances in Enzymology - And Related Areas of Molecular Biology

175

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The honour and opportunity of being invited to address you on the occasion of Professor Houtman's retirement is very much appreciated. However, having met him yesterday, I am convinced that I am not here to help celebrate his retirement as much as to initiate his new career.Just like careers, the role of metals in biology can be viewed from multiple points of view. In the past, metals have variously been thought to be beneficial, toxic or to serve no purpose at all in biology. It is not very long ago that documentation for the validity of all th ree perceptions seemed to coexist, and that they had equally vigorous advocates; but by now the hypothesis that they serve no biological purpose has faded into oblivion. This dilemma owed much to the fact that many metals are present in 'trace' amounts. I want to address myself today to the general principles underlying the evolution of metallobiochemistry and of its subdisciplines which did not exist a generation ago and give perspective to metals as toxic, environmental agents, a subject which has been of special interest to Prof. Houtman.The word 'trace' implies something that can be measured qualitatively but not quantitatively, and until about a generation ago that was true for many metals in biology. Therefore it was a nearly mystical subject explored of ten by individuals who had ideas about the problem but who performed few experiments to verify or reject them. This has changed. Measurement of very low concentrations of metals in biology has become quite routine. Technical problems have been eliminated to the point where the term 'trace' has become meaningless. That is fortunate, indeed, because to many 'trace' also meant 'unimportant' or 'insignificant' .Attention to the detection limits of analytical methods for metals has become almost irrelevant now. Yet, the fact that the II-B metals and those of the first transition series all occur in biological matter in similarly low concentrations led to the tacit inference that all of them would be found to perform similar functions. Such an emphasis on similarities of concentrations completely ignored the chemical properties of metals which are unique for each. Not too surprisingly, their biological roles have turned out to be as characteristic as their chemistries, enhanced by co-ordination of metals with 132 12 (1988) DELFT PROGRESS REPORT

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Section: The Metallobiochemistry Of Zinc Enzymes 403mentioning

confidence: 93%

Section: The Metallobiochemistry Of Zinc Enzymes 403mentioning

confidence: 95%

The Metallobiochemistry of Zinc Enzymes

Vallée

Galdes

1984

Advances in Enzymology - And Related Areas of Molecular Biology

175

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“…These binding sites are arranged in two separate polynuclear clusters, containing three and four metal ions respectively. Seven distinct cadmium environments have been indicated for rat MT-II (Sadler et al, 1978), although binding of a full complement of seven Cd and Zn atoms has been difficult to demonstrate (cf. Winge & Miklossy, 1982;Kagi et al, 1974).…”

Section: Discussionmentioning

confidence: 99%

Chemical modifications of metallothionein. Preparation and characterization of polymers

Templeton¹,

Cherian²

1984

Biochemical Journal

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Reaction of rat liver metallothionein-II with two bifunctional cross-linking reagents, glutaraldehyde and dimethyl suberimidate, produces high yields of polymeric species. It is argued that cross-linking is trapping preformed aggregates of the protein, which therefore represent a stabilized quaternary structure of metallothionein. The two polymeric species differ in a number of respects. With dimethyl suberimidate, the polymer retains all metal-binding sites of the monomer, and has an unaltered isoelectric point. Reaction with glutaraldehyde causes loss of one or two Cd2+/Zn2+-binding sites and elevates the pI. Both species are nearly spherical aggregates, in contrast with the highly asymmetrical metallothionein. Both polymers are linked through lysine residues, and the thiol groups remain reduced. The biological significance of these aggregates is discussed.

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“…The potential of Fourier Transform "'Cd nmr for the study of cadmium complexes in solution has already been amply demonstrated (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16). There is general agreement, however, that a lack of good "fingerprint" data on well-defined species is holding back development in this area ( 7 , 13-15).…”

Section: Introductionmentioning

confidence: 99%

A ³¹P nuclear magnetic resonance spectroscopic study of complexes of cadmium(II) with some phosphine oxides, sulfides, and selenides

Dean¹,

Hughes²

1980

Can. J. Chem.

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the ligands Ph,PE (E = S or Se). PhZP(E)(CH,),,P(E)Ph2 ( n = 1 or 2, E = 0. S or Se; n = 3. E = Se). [Ph,P(E)CH,],CMe (E = S or Se) and Ph2P(E)(CH,),PPh(E)(CH,),P(E)PhZ (E = 0, S , or Se) in liquid SOZ has been studied. mainly by low-temperature "P nmr spectroscopy. With the sulfides and selenides the maximum donor atom/Cd ratio observed is four. as shown by the limiting lou temperature spectra of (Ph3PE),Cd2+ (E = S or Se). [CH2(PPh2(Se))l]ZCd", and [PhZP(E)CH2CMe(CH2PPh2(E))2]2CdZ+ (E = S or Se). The laht two complexes both contain apotentially tridentate ligand behaving in a bidentate manner and their spectra are unexpectedly complicated due, perhaps. to conformational effects. Slow exchange spectra of [Ph2P(E)(CH2)2PPh(E)(CH2)2PPh2(E)]CdZ-( E = S or Se) show that in each complex the ligand behaves in a tridentate manner. For the preceding complexes. two-bond l"ll"Cd-'lP coupling is observed at the donor sites. and for the selenides a reduction in 1 1~( 3 '~-7 7~e ) l on complexation further identifies the bound -PSe groups. The maximum coordination number appears to be six in the complexes of the phosphine oxides. Both 2: 1 and 3: 1 L:Cd complexes exist for both of the bidentate ligands Ph2P(0)(CH2),,P(O)Ph2 (rr = I or 2) whereas in the system Ph,P(O) (CH2)2P(0) Ph(CHZ),P(O)Ph,-Cd2-the species identified is the presumably six-coordinate 2: 1 complex. For comparison, the six-coordinate complex [{CHZ(PPh2(0))2}3Hg]2' has been identified in solution also.Competition studies between the dioxides. disulfides. and diselenides ofthe diphosphines show that the disulfides and diselenides cannot compete \+ith the dioxides for cadmium. but that the diselenides can compete with the disulfides to a limited extent.

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¹¹³Cd nuclear magnetic resonance of metallothionein

Cited by 39 publications

References 10 publications

The Metallobiochemistry of Zinc Enzymes

The Metallobiochemistry of Zinc Enzymes

Chemical modifications of metallothionein. Preparation and characterization of polymers

A ³¹P nuclear magnetic resonance spectroscopic study of complexes of cadmium(II) with some phosphine oxides, sulfides, and selenides

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113Cd nuclear magnetic resonance of metallothionein

Cited by 39 publications

References 10 publications

The Metallobiochemistry of Zinc Enzymes

The Metallobiochemistry of Zinc Enzymes

Chemical modifications of metallothionein. Preparation and characterization of polymers

A 31P nuclear magnetic resonance spectroscopic study of complexes of cadmium(II) with some phosphine oxides, sulfides, and selenides

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¹¹³Cd nuclear magnetic resonance of metallothionein

A ³¹P nuclear magnetic resonance spectroscopic study of complexes of cadmium(II) with some phosphine oxides, sulfides, and selenides