Interaction of nitric oxide with the oxygen evolving complex of photosystem II and manganese catalase: A comparative study

Nikolaos Ioannidis, Gert Schansker, Vladimir V. Barynin, Vasili Petrouleas

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We compare the interaction of nitric oxide with the S states of the oxygen evolving complex (OEC) of photosystem II and the dinuclear Mn cluster of Thermus thermophilus catalase. Flash fluorescence studies indicate that the S3 state of the OEC in the presence of ca. 0.6 mM NO is reduced to the S1 with an apparent halftime of ca. 0.4 s at about 18 °C, compared with a biphasic decay, with approximate halftimes of 28 s for S3 to S2 and 140 s for S2 to S1 in the absence of NO. Under similar conditions the S2 state is reduced by NO to the S1 state with an approximate halftime of 2 s. These results extend a recent study indicating a slow reduction of the S1 state at -30°C, via the S0 and S-1 states, to a Mn(II)-Mn(III) state resembling the corresponding state in catalase. The reductive mode of action of NO is repeated with the di-Mn cluster of catalase: the Mn(III)-Mn(III) redox state is reduced to the Mn(II)-Mn(II) state via the intermediate Mn(II)-Mn(III) state. The kinetics of this reduction suggest a decreasing reduction potential with decreasing oxidation state, similar to what is observed with the active states of the OEC. What is unique about the OEC is the rapid interaction of NO with the S3 state of the OEC, which is compatible with a metalloradical character of this state.

Original languageEnglish
Pages (from-to)354-363
Number of pages10
JournalJournal of Biological Inorganic Chemistry
Issue number3
Publication statusPublished - Jun 2000



  • Catalase
  • Manganese cluster
  • Nitric oxide
  • Photosystem II

ASJC Scopus subject areas

  • Biochemistry
  • Inorganic Chemistry

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