Cleavage of Human Orosomucoid by a Chromium(V) Species: Relevance in Biotoxicity of Chromium

Shrivastava, H. Yamini; Nair, Balachandran Unni

doi:10.1006/bbrc.2000.4047

Cited by 16 publications

(14 citation statements)

References 25 publications

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“…Early studies in the area of metal-promoted peptide cleavage employed metal complexes in combination with oxidoreductive additives to achieve either oxidative (68)(69)(70)(71)(72)(73)(74)(75)(76)(77)(78)(79)(80)(81)(82) Metal complexes [e.g., a Cu(I) complex of 1,10-phenanthroline (phen) or and Fe(II) complex of ethylenediaminetetraacetato (edta, ligand)] conjugated to deoxyribonucleic acid (DNA) binding ligands oxidatively cleave nucleic acids in the presence of redox additives (84,85). The redox chemistry of those coordination complexes is related to the oxidative cleavage of polypeptide backbones of proteins.…”

Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Chei¹,

Suh²

2007

Progress in Inorganic Chemistry

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Section: A Agents For Oxidative Cleavage Of Proteinsmentioning

confidence: 99%

Peptide‐ or Protein‐Cleaving Agents Based on Metal Complexes

Chei¹,

Suh²

2007

Progress in Inorganic Chemistry

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“…Metal ions and complexes are used to effect cleavage of the polypeptide backbone under nondenaturing conditions of temperature and pH [34][35][36]41,[44][45][46][47][48][49][50][51][52]. Because mild conditions can be employed, these reagents show great promise for use in the analysis of protein solution structure, in protein engineering (e.g., the generation of semi-synthetic proteins, the proteolytic cleavage of bioengineered fusion proteins), and in therapeutics.…”

mentioning

confidence: 99%

“…Redox active metal ions and/or complexes of Cu II [3,7,17,21,44], Cr III [45], Cr V [46], Fe III [1,2,[4][5][6]8,9,11,13,14,16,18,19,21,22,[24][25][26][27][28], Ni II [23], Rh III [11], and V V [10,12,15,20] have been used to promote the oxidative cleavage of peptide amide bonds in folded proteins under nondenaturing conditions. In the majority of cases (e.g., Cu II , Cr III , Cr V , Fe III , and V V ), cleavage is thought to arise from abstraction of peptide backbone α-carbon hydrogen atoms by hydroxyl radicals and other metal-generated, reactive oxygen species [45,[53][54][55][56].…”

mentioning

confidence: 99%

Major Advances in the Hydrolysis of Peptides and Proteins by Metal Ions and Complexes

Grant¹,

Kassai

2006

COC

116

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Metal ions and complexes that hydrolyze peptides and proteins have become increasingly important in recent years. These reagents have shown great promise for use in a variety of applications including protein sequencing and proteomics. When metal-assisted hydrolytic cleavage is accomplished under nondenaturing conditions of temperature and pH, their use can be extended to include the study of protein function and solution structure, the generation of semisynthetic proteins, the proteolytic cleavage of bioengineered fusion proteins, and therapeutics. Yet, because of the extreme stability of the peptide amide bond, hydrolytically active metals are limited in number and there is now great interest in the development of new, more efficient reagents. In this review, we provide a description of relevant, early work with metal ions and complexes that have been used to hydrolyze unactivated peptide amide bonds in peptides and proteins. More importantly, we present an overview of recent contributions that have been made toward the development of synthetic metalloproteases that catalyze hydrolysis under near physiological conditions of temperature and pH.Dedicated to Professor Koji Nakanishi on the occasion of his 80 th birthday.

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“…4), which confirms the formation of chromium(V) species. Chromium(V) species has previously been shown to cleave alpha 1 -acid glycoproteins [21]. Hence, it is clear that the chromium(V)nitrido species oxidatively cleaves the protein.…”

Section: Resultsmentioning

confidence: 99%