Model compounds for metal–protein interaction: crystal structure of three platinum(<scp>II</scp>) complexes of<scp>L</scp>- and<scp>DL</scp>-methionine and glycyl-<scp>L</scp>-methionine

Freeman, H.C.; Golomb, M. L.

doi:10.1039/c29700001523

Cited by 75 publications

(48 citation statements)

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“…* Discussion. The crystals of (I) used in the present work belong to the monoclinic space group P2~; those used in the original structure analysis belonged to the triclinic space group P1 (Freeman & Golomb, 1970). The volume of the monoclinic cell is twice the volume of the previously reported triclinic cell, but there are no other obvious relationships between the two cells.…”

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confidence: 75%

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Structures of dichloro[(S)-methionine-N,S]platinum(II) and chloro[glycyl-(S)-methioninato-N,N',S]platinum(II) monohydrate

Wilson¹,

Scudder²,

Hambley³

et al. 1992

Acta Crystallogr C

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confidence: 75%

“…The structures of dichloro-(S)-methionineplatinum(II), (I), and of chloroglycl-(S)-methioninatoplatinum(II) monohydrate, (II), were reported in a preliminary publication by Freeman & Golomb (1970). We have redetermined these structures using high-resolution data.…”

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confidence: 99%

Structures of dichloro[(S)-methionine-N,S]platinum(II) and chloro[glycyl-(S)-methioninato-N,N',S]platinum(II) monohydrate

Wilson¹,

Scudder²,

Hambley³

et al. 1992

Acta Crystallogr C

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“…Thus, the methionine compounds listed in Table 4.7 are actually not amino acid salts. In these compounds, the amino acids act as bidentate (N,S) ligands, as shown for dichloro-(L-methionine)-platinum (Freeman and Golomb 1970; the respective D-form was reported by Llorca et al 2001; Fig. 4.17).…”

Section: Proline Methionine Phenylalanine and Tryptophanmentioning

confidence: 93%

Compounds of Amino Acids and Neutral Salts

Fleck

Petrosyan

2014

Salts of Amino Acids

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In this chapter we present salts composed of amino acids combined with inorganic cations and anions. These salts generally contain amino acids in neutral, i.e., zwitterionic form, with the charges balanced by the cations and anions. However, some of the phases resented here contain cations, anions, and amino acids, but the amino acids are not in neutral form, as, e.g., glycinate À Cu, but for reasons of similarity, they are included in this chapter. The variation of salts (and thus the number of species) is even greater as for salts of amino acids and cations, as a multitude of combinations of amino acids, cations, and anions is possible. Additionally, different hydration states are often found, as well as different ratios of components. Thus, there are several instances of systems containing more than one phase (e.g., the system glycine-zinc-chloride-water). Despite the greater variation, many coordination patterns found in the salts described in the previous chapter recur in the salts reported here. Likewise, the connectivities of units are similar as those found in salts of amino acids and cations. Instances of materials with noteworthy physical properties are presented. Keywords Introducing RemarksAs stated before, this chapter deals with salts of amino acids and neutral, inorganic salts. In these species, the amino acid usually exists in zwitterionic form, but it is still coordinated to a cation. As other anions are present, the amino acids are not the only possible ligands. These anions can act as additional ligands (plus possible water molecules as well). Moreover, in some cases the inorganic anions are not part of the coordination spheres, but located in the interstices between units composed of cations and coordinating amino acids.M. Fleck and A.M. Petrosyan, Salts of Amino Acids: Crystallization, Structure and Properties,

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“…The labeling reagent used was the dark form of a complex between the dipeptide glycyl-L-methionine and Pt (16). The structure of a related compound is known (17). The resinous product (Gly-Met-Pt) of the synthesis was solubilized for reaction with purple membranes by placing it in 1 M NaOH, and this solution was then titrated to the reaction pH with HC1…”

Section: Methodsmentioning

confidence: 99%

Location of platinum binding sites on bacteriorhodopsin by electron diffraction

Dumont

Wiggins

Hayward

1981

Proc. Natl. Acad. Sci. U.S.A.

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A platinum-containing derivative of bacteriorhodopsin has been prepared by treating purple membranes with glycyl-L-methionatoplatinum. Low-dose electron diffraction was used to identify Pt binding sites in the 5.6 A resolution reconstruction of the bacteriorhodopsin unit cell in projection. This is a necessary first step in the use of the Pt derivative for identifying the parts of the amino acid sequence corresponding to the a helices in the bacteriorhodopsin structure and for obtaining phases for reflections out to 3.5 A resolution by the method of heavy-atom isomorphous replacement. The largest peak in a Fourier difference map between platinum-labeled and native purple membrane is larger than the spurious features expected to arise from errors in measurements of diffraction intensities.A number ofproteins that have biologically interesting'functions have been found to be capable offorming two-dimensional crystalline arrays, but not, as ofyet, well-ordered three-dimensional crystals (1-6). Electron diffraction and electron imaging have been used in the structural analyses of these proteins because of the difficulty of obtaining single-crystal x-ray diffraction patterns from two-dimensional small crystals. We discuss here the use of single heavy-atom labels for obtaining detailed structural information from two-dimensional arrays, using as a demonstration our studies ofPt binding to bacteriorhodopsin (BR), the light-driven proton pump from the purple membrane fraction of Halobacterium halobium.The tendency ofBR to form two-dimensional crystals allowed Henderson and Unwin to use low-dose electron imaging and diffraction to determine the three-dimensional structure of the molecule to 7 A resolution (1, 7). Two main factors have blocked the extension ofthis structural study to higher resolution. First, it has been difficult to obtain significant intensity in high-resolution diffraction orders. Because purple membranes are ordered to at least 3.5 A resolution (8), intensity is limited by the low levels of electron irradiation that can be tolerated without destruction of the specimen and by the small size of the crystalline membrane patches. Second, currently available electron imaging systems are incapable ofachieving 3.5 A resolution over large specimen areas without distortion (9).As the amino acid sequence of BR is known (10, 11), one way to get a detailed understanding of BR chain folding is to attach heavy atoms to known amino acids in the sequence and use electron diffraction to locate the heavy atoms in the low-resolution structure. The high a helix content of the protein has already led to some model building efforts (12), a major remaining uncertainty being the question of which part of the sequence is identified with each a helical segment in the structural map.

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Model compounds for metal–protein interaction: crystal structure of three platinum(II) complexes ofL- andDL-methionine and glycyl-L-methionine

Cited by 75 publications

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Structures of dichloro[(S)-methionine-N,S]platinum(II) and chloro[glycyl-(S)-methioninato-N,N',S]platinum(II) monohydrate

Structures of dichloro[(S)-methionine-N,S]platinum(II) and chloro[glycyl-(S)-methioninato-N,N',S]platinum(II) monohydrate

Compounds of Amino Acids and Neutral Salts

Location of platinum binding sites on bacteriorhodopsin by electron diffraction

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