Recognition of cytochrome C by tetraphenylporphyrin-based protein surface receptors

Rishi K. Jain; Lun K. Tsou; Andrew D. Hamilton

doi:10.1007/1-4020-3687-6_17

Recognition of cytochrome C by tetraphenylporphyrin-based protein surface receptors

Rishi K. Jain, Lun K. Tsou, Andrew D. Hamilton

Chemistry

Research output: Chapter in Book/Report/Conference proceeding › Chapter

Abstract

Cytochrome c (cyt. c) has become a major protein for testing new approaches and techniques in protein science.1 This is partly due to the venerable position that cytochrome c holds in the field of biochemistry since it was isolated and characterized more than 70 years ago. Cyt. c was one of the first proteins to be sequenced,² and to have its X-ray structure determined in 1967.³ Cyt. c also has the advantage of stability and a spectroscopically distinct heme group. More than 23,000 articles mentioning cyt. c were published between 1945-2002 (ISI Web of Science). Here, we describe an approach to tetraphenylporphyrin-based protein surface receptors and the characterization of their interactions with the principal target cyt. c.

Original language	English (US)
Title of host publication	Macrocyclic Chemistry
Subtitle of host publication	Current Trends and Future Perspectives
Publisher	Springer Netherlands
Pages	267-275
Number of pages	9
ISBN (Print)	1402033648, 9781402033643
DOIs	https://doi.org/10.1007/1-4020-3687-6_17
State	Published - 2005

ASJC Scopus subject areas

General Materials Science
General Chemistry

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10.1007/1-4020-3687-6_17

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title = "Recognition of cytochrome C by tetraphenylporphyrin-based protein surface receptors",

abstract = "Cytochrome c (cyt. c) has become a major protein for testing new approaches and techniques in protein science.1 This is partly due to the venerable position that cytochrome c holds in the field of biochemistry since it was isolated and characterized more than 70 years ago. Cyt. c was one of the first proteins to be sequenced,2 and to have its X-ray structure determined in 1967.3 Cyt. c also has the advantage of stability and a spectroscopically distinct heme group. More than 23,000 articles mentioning cyt. c were published between 1945-2002 (ISI Web of Science). Here, we describe an approach to tetraphenylporphyrin-based protein surface receptors and the characterization of their interactions with the principal target cyt. c.",

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year = "2005",

doi = "10.1007/1-4020-3687-6_17",

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AU - Jain, Rishi K.

AU - Tsou, Lun K.

AU - Hamilton, Andrew D.

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N2 - Cytochrome c (cyt. c) has become a major protein for testing new approaches and techniques in protein science.1 This is partly due to the venerable position that cytochrome c holds in the field of biochemistry since it was isolated and characterized more than 70 years ago. Cyt. c was one of the first proteins to be sequenced,2 and to have its X-ray structure determined in 1967.3 Cyt. c also has the advantage of stability and a spectroscopically distinct heme group. More than 23,000 articles mentioning cyt. c were published between 1945-2002 (ISI Web of Science). Here, we describe an approach to tetraphenylporphyrin-based protein surface receptors and the characterization of their interactions with the principal target cyt. c.

AB - Cytochrome c (cyt. c) has become a major protein for testing new approaches and techniques in protein science.1 This is partly due to the venerable position that cytochrome c holds in the field of biochemistry since it was isolated and characterized more than 70 years ago. Cyt. c was one of the first proteins to be sequenced,2 and to have its X-ray structure determined in 1967.3 Cyt. c also has the advantage of stability and a spectroscopically distinct heme group. More than 23,000 articles mentioning cyt. c were published between 1945-2002 (ISI Web of Science). Here, we describe an approach to tetraphenylporphyrin-based protein surface receptors and the characterization of their interactions with the principal target cyt. c.

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M3 - Chapter

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SN - 9781402033643

SP - 267

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BT - Macrocyclic Chemistry

PB - Springer Netherlands

ER -

Recognition of cytochrome C by tetraphenylporphyrin-based protein surface receptors

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