Phosphorylation of tyrosine enhances its electron transfer capability: A model of redox modulation as oncogene expression?

D. A. Peterson; B. Kelly; J. Butterfield; J. Ashley; R. Peterson; J. M. Gerrard

doi:10.1016/0306-9877(88)90133-8

Phosphorylation of tyrosine enhances its electron transfer capability: A model of redox modulation as oncogene expression?

D. A. Peterson, B. Kelly, J. Butterfield, J. Ashley, R. Peterson, J. M. Gerrard

Medicine - Veteran's Administration Medical Center

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

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Abstract

The influence of tyrosine and o-phosphotyrosine on the transfer of electrons to nitrobluetetrazolium (NBT) was studied. Tyrosine phosphate was found to strongly promote the transfer of electrons from ferrous iron to NBT, while tyrosine was inhibitory. The enhancement of NBT reduction by tyrosine phosphate was blocked by superoxide dismutase (SOD). The results suggest a role for phosphorylated tyrosine residues to promote intracellular redox reactions. We suggest that the role of tyrosine protein kinases in cell proliferation and transformation may be to regulate electron transport in as yet undefined cellular systems. Consistent with a unique role for phosphotyrosine, the other commonly occurring phosphoamino acids, o-phosphoserine and o-phosphothreonine were not effective electron transfer agents.

Original language	English (US)
Pages (from-to)	271-273
Number of pages	3
Journal	Medical Hypotheses
Volume	26
Issue number	4
DOIs	https://doi.org/10.1016/0306-9877(88)90133-8
State	Published - Aug 1988

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title = "Phosphorylation of tyrosine enhances its electron transfer capability: A model of redox modulation as oncogene expression?",

abstract = "The influence of tyrosine and o-phosphotyrosine on the transfer of electrons to nitrobluetetrazolium (NBT) was studied. Tyrosine phosphate was found to strongly promote the transfer of electrons from ferrous iron to NBT, while tyrosine was inhibitory. The enhancement of NBT reduction by tyrosine phosphate was blocked by superoxide dismutase (SOD). The results suggest a role for phosphorylated tyrosine residues to promote intracellular redox reactions. We suggest that the role of tyrosine protein kinases in cell proliferation and transformation may be to regulate electron transport in as yet undefined cellular systems. Consistent with a unique role for phosphotyrosine, the other commonly occurring phosphoamino acids, o-phosphoserine and o-phosphothreonine were not effective electron transfer agents.",

author = "Peterson, {D. A.} and B. Kelly and J. Butterfield and J. Ashley and R. Peterson and Gerrard, {J. M.}",

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T1 - Phosphorylation of tyrosine enhances its electron transfer capability

T2 - A model of redox modulation as oncogene expression?

AU - Peterson, D. A.

AU - Kelly, B.

AU - Butterfield, J.

AU - Ashley, J.

AU - Peterson, R.

AU - Gerrard, J. M.

PY - 1988/8

Y1 - 1988/8

N2 - The influence of tyrosine and o-phosphotyrosine on the transfer of electrons to nitrobluetetrazolium (NBT) was studied. Tyrosine phosphate was found to strongly promote the transfer of electrons from ferrous iron to NBT, while tyrosine was inhibitory. The enhancement of NBT reduction by tyrosine phosphate was blocked by superoxide dismutase (SOD). The results suggest a role for phosphorylated tyrosine residues to promote intracellular redox reactions. We suggest that the role of tyrosine protein kinases in cell proliferation and transformation may be to regulate electron transport in as yet undefined cellular systems. Consistent with a unique role for phosphotyrosine, the other commonly occurring phosphoamino acids, o-phosphoserine and o-phosphothreonine were not effective electron transfer agents.

AB - The influence of tyrosine and o-phosphotyrosine on the transfer of electrons to nitrobluetetrazolium (NBT) was studied. Tyrosine phosphate was found to strongly promote the transfer of electrons from ferrous iron to NBT, while tyrosine was inhibitory. The enhancement of NBT reduction by tyrosine phosphate was blocked by superoxide dismutase (SOD). The results suggest a role for phosphorylated tyrosine residues to promote intracellular redox reactions. We suggest that the role of tyrosine protein kinases in cell proliferation and transformation may be to regulate electron transport in as yet undefined cellular systems. Consistent with a unique role for phosphotyrosine, the other commonly occurring phosphoamino acids, o-phosphoserine and o-phosphothreonine were not effective electron transfer agents.

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JO - Medical Hypotheses

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ER -

Phosphorylation of tyrosine enhances its electron transfer capability: A model of redox modulation as oncogene expression?

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