Proximity of the manganese cluster of photosystem II to the redox-active tyrosine YZ.

Abstract:

:Electron spin echo electron-nuclear double resonance (ESE-ENDOR) experiments performed on a broad radical electron paramagnetic resonance (EPR) signal observed in photosystem II particles depleted of Ca2+ indicate that this signal arises from the redox-active tyrosine YZ. The tyrosine EPR signal width is increased relative to that observed in a manganese-depleted preparation due to a magnetic interaction between the photosystem II manganese cluster and the tyrosine radical. The manganese cluster is located asymmetrically with respect to the symmetry-related tyrosines YZ and YD. The distance between the YZ tyrosine and the manganese cluster is estimated to be approximately 4.5 A. Due to this close proximity of the Mn cluster and the redox-active tyrosine YZ, we propose that this tyrosine abstracts protons from substrate water bound to the Mn cluster.

authors

Gilchrist ML Jr,Ball JA,Randall DW,Britt RD

doi

10.1073/pnas.92.21.9545

subject

Has Abstract

pub_date

1995-10-10 00:00:00

pages

9545-9

issue

21

eissn

0027-8424

issn

1091-6490

journal_volume

92

pub_type

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