Direct comparison of electron transfer properties of two distinct semisynthetic triads with non-protein based triad

Unambiguous experimental evidences on protein matrix effects

Yi Zhen Hu, Hiroshi Takashima, Shinya Tsukiji, Seiji Shinkai, Teruyuki Nagamune, Shigero Oishi, Itaru Hamachi

Research output: Contribution to journalReview article

40 Citations (Scopus)

Abstract

In order to understand the roles of protein matrix in electron transfer processes (ET) within biological systems, a heme-based donor (Zn-heme: ZnPP)-sensitizer (Ru2+(bpy)3)-acceptor (cyclic viologen: BXV4+) triad 1 was used as a probe molecule. Two semisynthetic systems, Cyt-b562(1) and Mb(1), in which the triad is incorporated into cytochrome b562 (Cyt-b562) or into myoglobin (Mb), were constructed by cofactor reconstitution. These two semisynthetic proteins were compared with the triad itself (i.e., without the protein matrix) using absorption spectroscopy, steady state emission and excitation studies, laser flash photolysis experiments, and molecular modeling. Photoexcitation of the ZnPP moiety of Cyt-b562(1) or Mb(1) leads to a direct ET from the triplet state of ZnPP state (3ZnPP) to BXV4+ to generate a final charge-separated (CS) state, Cyt-b562(Zn+)-Ru2+-BXV3+• or Mb(Zn+)-Ru2+-BXV3+•. On the other hand, direct ET from the excited ZnPP moiety to the BXV4+ moiety is also involved in 1 in the absence of the protein matrix, but the excited state of ZnPP involved is not 3ZnPP, but the singlet excited state (1ZnPP) in this pathway. When the Ru2+(bpy)3 moiety of Cyt-b562(1) or Mb(1) is excited, a stepwise ET relay occurs with the ion-pair, Cyt-b562(Zn)-Ru3+-BXV3+• or Mb(Zn)-Ru3+-BXV3+•, as an intermediate, leading to the same final CS state as that generated in the direct ET pathway. The lifetimes of the corresponding final CS states were determined to be 300 ns for 1 in the absence of the protein matrix, 600-900ns for Cyt-b562(1) and 1.1-18 μs for Mb(1), the values of which are greatly affected by the protein matrix. Molecular modeling study of the three systems consistently explained the differences of their photophysical behavior.

Original languageEnglish
Pages (from-to)1907-1916
Number of pages10
JournalChemistry - A European Journal
Volume6
Issue number11
DOIs
Publication statusPublished - Jun 2 2000

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Myoglobin
Cytochromes
Proteins
Electrons
Molecular modeling
Heme
Excited states
Viologens
Photoexcitation
Photolysis
Biological systems
Absorption spectroscopy
Ions
Molecules
Lasers

All Science Journal Classification (ASJC) codes

  • Chemistry(all)

Cite this

Direct comparison of electron transfer properties of two distinct semisynthetic triads with non-protein based triad : Unambiguous experimental evidences on protein matrix effects. / Hu, Yi Zhen; Takashima, Hiroshi; Tsukiji, Shinya; Shinkai, Seiji; Nagamune, Teruyuki; Oishi, Shigero; Hamachi, Itaru.

In: Chemistry - A European Journal, Vol. 6, No. 11, 02.06.2000, p. 1907-1916.

Research output: Contribution to journalReview article

Hu, Yi Zhen ; Takashima, Hiroshi ; Tsukiji, Shinya ; Shinkai, Seiji ; Nagamune, Teruyuki ; Oishi, Shigero ; Hamachi, Itaru. / Direct comparison of electron transfer properties of two distinct semisynthetic triads with non-protein based triad : Unambiguous experimental evidences on protein matrix effects. In: Chemistry - A European Journal. 2000 ; Vol. 6, No. 11. pp. 1907-1916.
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abstract = "In order to understand the roles of protein matrix in electron transfer processes (ET) within biological systems, a heme-based donor (Zn-heme: ZnPP)-sensitizer (Ru2+(bpy)3)-acceptor (cyclic viologen: BXV4+) triad 1 was used as a probe molecule. Two semisynthetic systems, Cyt-b562(1) and Mb(1), in which the triad is incorporated into cytochrome b562 (Cyt-b562) or into myoglobin (Mb), were constructed by cofactor reconstitution. These two semisynthetic proteins were compared with the triad itself (i.e., without the protein matrix) using absorption spectroscopy, steady state emission and excitation studies, laser flash photolysis experiments, and molecular modeling. Photoexcitation of the ZnPP moiety of Cyt-b562(1) or Mb(1) leads to a direct ET from the triplet state of ZnPP state (3ZnPP) to BXV4+ to generate a final charge-separated (CS) state, Cyt-b562(Zn+)-Ru2+-BXV3+• or Mb(Zn+)-Ru2+-BXV3+•. On the other hand, direct ET from the excited ZnPP moiety to the BXV4+ moiety is also involved in 1 in the absence of the protein matrix, but the excited state of ZnPP involved is not 3ZnPP, but the singlet excited state (1ZnPP) in this pathway. When the Ru2+(bpy)3 moiety of Cyt-b562(1) or Mb(1) is excited, a stepwise ET relay occurs with the ion-pair, Cyt-b562(Zn)-Ru3+-BXV3+• or Mb(Zn)-Ru3+-BXV3+•, as an intermediate, leading to the same final CS state as that generated in the direct ET pathway. The lifetimes of the corresponding final CS states were determined to be 300 ns for 1 in the absence of the protein matrix, 600-900ns for Cyt-b562(1) and 1.1-18 μs for Mb(1), the values of which are greatly affected by the protein matrix. Molecular modeling study of the three systems consistently explained the differences of their photophysical behavior.",
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