Site-specific hydrolysis of horse heart cytochrome c and apocytochrome c promoted by palladium(II) complex

Feng Qiao; Jianzhong Hu; Haizhong Zhu; Xuemei Luo; Longgen Zhu; Dexu Zhu

doi:10.1016/S0277-5387(99)00037-6

Site-specific hydrolysis of horse heart cytochrome c and apocytochrome c promoted by palladium(II) complex

Feng Qiao, Jianzhong Hu, Haizhong Zhu, Xuemei Luo, Longgen Zhu, Dexu Zhu

Research output: Contribution to journal › Article › peer-review

17 Scopus citations

Abstract

Horse heart cytochrome c and apocytochrome c (with the Fe-porphyrin removed), which have completely different conformations, are selectively cleaved at the same site in the presence of cis-[Pd(dtco-3-OH)(H₂O)₂]²⁺ (dtco-3-OH=dithiacycrooctan-3-ol). The cleaved fragments were separated by SDS-polyacrylamide gel electrophoresis and the cleavage yields were determined by a scanning densitometer. The site and size of cleavage were confirmed by precisely determining molecular masses of the proteins and of the cleaved fragments using electrospray mass spectrometry. Different pH behavior in the cleavage of cytochrome c and apocytochrome c is observed due to a requirement of a partially unfolded state II of the cytochrome c. Although the Pd(II) complex coordinates to different sulfur forms of Cys17 in the cytochrome c and the apocytochrome c (thioether in the former and thiolate anion in the latter), their cleavage yields at pH<2 are comparable.

Original language	English
Pages (from-to)	1629-1633
Number of pages	5
Journal	Polyhedron
Volume	18
Issue number	11
DOIs	https://doi.org/10.1016/S0277-5387(99)00037-6
State	Published - 16 Apr 1999
Externally published	Yes

Keywords

Apocytochrome c
Cytochrome c
Palladium
Protein cleavage

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10.1016/S0277-5387(99)00037-6

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@article{fb136475af92477e96bb65f8321d5a23,

title = "Site-specific hydrolysis of horse heart cytochrome c and apocytochrome c promoted by palladium(II) complex",

abstract = "Horse heart cytochrome c and apocytochrome c (with the Fe-porphyrin removed), which have completely different conformations, are selectively cleaved at the same site in the presence of cis-[Pd(dtco-3-OH)(H2O)2]2+ (dtco-3-OH=dithiacycrooctan-3-ol). The cleaved fragments were separated by SDS-polyacrylamide gel electrophoresis and the cleavage yields were determined by a scanning densitometer. The site and size of cleavage were confirmed by precisely determining molecular masses of the proteins and of the cleaved fragments using electrospray mass spectrometry. Different pH behavior in the cleavage of cytochrome c and apocytochrome c is observed due to a requirement of a partially unfolded state II of the cytochrome c. Although the Pd(II) complex coordinates to different sulfur forms of Cys17 in the cytochrome c and the apocytochrome c (thioether in the former and thiolate anion in the latter), their cleavage yields at pH<2 are comparable.",

keywords = "Apocytochrome c, Cytochrome c, Palladium, Protein cleavage",

author = "Feng Qiao and Jianzhong Hu and Haizhong Zhu and Xuemei Luo and Longgen Zhu and Dexu Zhu",

note = "Funding Information: We thank the National Natural Science Foundation of China (Grant No. 29871017) and the Natural Science Foundation of Jiangsu Province (Grant No. 97015) for financial support.",

year = "1999",

month = apr,

day = "16",

doi = "10.1016/S0277-5387(99)00037-6",

language = "English",

volume = "18",

pages = "1629--1633",

journal = "Polyhedron",

issn = "0277-5387",

publisher = "Elsevier Ltd.",

number = "11",

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TY - JOUR

T1 - Site-specific hydrolysis of horse heart cytochrome c and apocytochrome c promoted by palladium(II) complex

AU - Qiao, Feng

AU - Hu, Jianzhong

AU - Zhu, Haizhong

AU - Luo, Xuemei

AU - Zhu, Longgen

AU - Zhu, Dexu

N1 - Funding Information: We thank the National Natural Science Foundation of China (Grant No. 29871017) and the Natural Science Foundation of Jiangsu Province (Grant No. 97015) for financial support.

PY - 1999/4/16

Y1 - 1999/4/16

N2 - Horse heart cytochrome c and apocytochrome c (with the Fe-porphyrin removed), which have completely different conformations, are selectively cleaved at the same site in the presence of cis-[Pd(dtco-3-OH)(H2O)2]2+ (dtco-3-OH=dithiacycrooctan-3-ol). The cleaved fragments were separated by SDS-polyacrylamide gel electrophoresis and the cleavage yields were determined by a scanning densitometer. The site and size of cleavage were confirmed by precisely determining molecular masses of the proteins and of the cleaved fragments using electrospray mass spectrometry. Different pH behavior in the cleavage of cytochrome c and apocytochrome c is observed due to a requirement of a partially unfolded state II of the cytochrome c. Although the Pd(II) complex coordinates to different sulfur forms of Cys17 in the cytochrome c and the apocytochrome c (thioether in the former and thiolate anion in the latter), their cleavage yields at pH<2 are comparable.

AB - Horse heart cytochrome c and apocytochrome c (with the Fe-porphyrin removed), which have completely different conformations, are selectively cleaved at the same site in the presence of cis-[Pd(dtco-3-OH)(H2O)2]2+ (dtco-3-OH=dithiacycrooctan-3-ol). The cleaved fragments were separated by SDS-polyacrylamide gel electrophoresis and the cleavage yields were determined by a scanning densitometer. The site and size of cleavage were confirmed by precisely determining molecular masses of the proteins and of the cleaved fragments using electrospray mass spectrometry. Different pH behavior in the cleavage of cytochrome c and apocytochrome c is observed due to a requirement of a partially unfolded state II of the cytochrome c. Although the Pd(II) complex coordinates to different sulfur forms of Cys17 in the cytochrome c and the apocytochrome c (thioether in the former and thiolate anion in the latter), their cleavage yields at pH<2 are comparable.

KW - Apocytochrome c

KW - Cytochrome c

KW - Palladium

KW - Protein cleavage

UR - http://www.scopus.com/inward/record.url?scp=0000469776&partnerID=8YFLogxK

U2 - 10.1016/S0277-5387(99)00037-6

DO - 10.1016/S0277-5387(99)00037-6

M3 - Article

AN - SCOPUS:0000469776

SN - 0277-5387

VL - 18

SP - 1629

EP - 1633

JO - Polyhedron

JF - Polyhedron

IS - 11

ER -

Site-specific hydrolysis of horse heart cytochrome c and apocytochrome c promoted by palladium(II) complex

Abstract

Keywords

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