A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina

Rei Narikawa, Takahiro Nakajima, Yuki Aono, Keiji Fushimi, Gen Enomoto, Ni Ni Win, Shigeru Itoh, Moritoshi Sato, Masahiko Ikeuchi

Research output: Contribution to journalArticle

45 Citations (Scopus)

Abstract

Cyanobacteriochromes (CBCRs) are linear tetrapyrrole-binding photoreceptors in cyanobacteria that absorb visible and near-ultraviolet light. CBCRs are divided into two types based on the type of chromophore they contain: phycocyanobilin (PCB) or phycoviolobilin (PVB). PCB-binding CBCRs reversibly photoconvert at relatively long wavelengths, i.e., the blue-to-red region, whereas PVB-binding CBCRs reversibly photoconvert at shorter wavelengths, i.e., the near-ultraviolet to green region. Notably, prior to this report, CBCRs containing biliverdin (BV), which absorbs at longer wavelengths than do PCB and PVB, have not been found. Herein, we report that the typical red/green CBCR AM1-1557 from the chlorophyll d-bearing cyanobacterium Acaryochloris marina can bind BV almost comparable to PCB. This BV-bound holoprotein reversibly photoconverts between a far red light-absorbing form (Pfr, Îλ max = 697 nm) and an orange light-absorbing form (Po, Î λ max = 622 nm). At room temperature, Pfr fluoresces with a maximum at 730 nm. These spectral features are red-shifted by 48∼77 nm compared with those of the PCB-bound domain. Because the absorbance of chlorophyll d is red-shifted compared with that of chlorophyll a, the BV-bound AM1-1557 may be a physiologically relevant feature of A. marina and is potentially useful as an optogenetic switch and/or fluorescence imager.

Original languageEnglish
Article number7950
JournalScientific reports
Volume5
DOIs
Publication statusPublished - Jan 22 2015

Fingerprint

Biliverdine
Cyanobacteria
Optogenetics
Tetrapyrroles
Light
Ultraviolet Rays
Fluorescence
chlorophyll d
phycocyanobilin
Temperature
phycoviolobilin

All Science Journal Classification (ASJC) codes

  • General

Cite this

A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina. / Narikawa, Rei; Nakajima, Takahiro; Aono, Yuki; Fushimi, Keiji; Enomoto, Gen; Win, Ni Ni; Itoh, Shigeru; Sato, Moritoshi; Ikeuchi, Masahiko.

In: Scientific reports, Vol. 5, 7950, 22.01.2015.

Research output: Contribution to journalArticle

Narikawa, R, Nakajima, T, Aono, Y, Fushimi, K, Enomoto, G, Win, NN, Itoh, S, Sato, M & Ikeuchi, M 2015, 'A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina', Scientific reports, vol. 5, 7950. https://doi.org/10.1038/srep07950
Narikawa, Rei ; Nakajima, Takahiro ; Aono, Yuki ; Fushimi, Keiji ; Enomoto, Gen ; Win, Ni Ni ; Itoh, Shigeru ; Sato, Moritoshi ; Ikeuchi, Masahiko. / A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina. In: Scientific reports. 2015 ; Vol. 5.
@article{d40bd13fdd034ca5aa58af93517c2b94,
title = "A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina",
abstract = "Cyanobacteriochromes (CBCRs) are linear tetrapyrrole-binding photoreceptors in cyanobacteria that absorb visible and near-ultraviolet light. CBCRs are divided into two types based on the type of chromophore they contain: phycocyanobilin (PCB) or phycoviolobilin (PVB). PCB-binding CBCRs reversibly photoconvert at relatively long wavelengths, i.e., the blue-to-red region, whereas PVB-binding CBCRs reversibly photoconvert at shorter wavelengths, i.e., the near-ultraviolet to green region. Notably, prior to this report, CBCRs containing biliverdin (BV), which absorbs at longer wavelengths than do PCB and PVB, have not been found. Herein, we report that the typical red/green CBCR AM1-1557 from the chlorophyll d-bearing cyanobacterium Acaryochloris marina can bind BV almost comparable to PCB. This BV-bound holoprotein reversibly photoconverts between a far red light-absorbing form (Pfr, {\^I}λ max = 697 nm) and an orange light-absorbing form (Po, {\^I} λ max = 622 nm). At room temperature, Pfr fluoresces with a maximum at 730 nm. These spectral features are red-shifted by 48∼77 nm compared with those of the PCB-bound domain. Because the absorbance of chlorophyll d is red-shifted compared with that of chlorophyll a, the BV-bound AM1-1557 may be a physiologically relevant feature of A. marina and is potentially useful as an optogenetic switch and/or fluorescence imager.",
author = "Rei Narikawa and Takahiro Nakajima and Yuki Aono and Keiji Fushimi and Gen Enomoto and Win, {Ni Ni} and Shigeru Itoh and Moritoshi Sato and Masahiko Ikeuchi",
year = "2015",
month = "1",
day = "22",
doi = "10.1038/srep07950",
language = "English",
volume = "5",
journal = "Scientific Reports",
issn = "2045-2322",
publisher = "Nature Publishing Group",

}

TY - JOUR

T1 - A biliverdin-binding cyanobacteriochrome from the chlorophyll d-bearing cyanobacterium Acaryochloris marina

AU - Narikawa, Rei

AU - Nakajima, Takahiro

AU - Aono, Yuki

AU - Fushimi, Keiji

AU - Enomoto, Gen

AU - Win, Ni Ni

AU - Itoh, Shigeru

AU - Sato, Moritoshi

AU - Ikeuchi, Masahiko

PY - 2015/1/22

Y1 - 2015/1/22

N2 - Cyanobacteriochromes (CBCRs) are linear tetrapyrrole-binding photoreceptors in cyanobacteria that absorb visible and near-ultraviolet light. CBCRs are divided into two types based on the type of chromophore they contain: phycocyanobilin (PCB) or phycoviolobilin (PVB). PCB-binding CBCRs reversibly photoconvert at relatively long wavelengths, i.e., the blue-to-red region, whereas PVB-binding CBCRs reversibly photoconvert at shorter wavelengths, i.e., the near-ultraviolet to green region. Notably, prior to this report, CBCRs containing biliverdin (BV), which absorbs at longer wavelengths than do PCB and PVB, have not been found. Herein, we report that the typical red/green CBCR AM1-1557 from the chlorophyll d-bearing cyanobacterium Acaryochloris marina can bind BV almost comparable to PCB. This BV-bound holoprotein reversibly photoconverts between a far red light-absorbing form (Pfr, Îλ max = 697 nm) and an orange light-absorbing form (Po, Î λ max = 622 nm). At room temperature, Pfr fluoresces with a maximum at 730 nm. These spectral features are red-shifted by 48∼77 nm compared with those of the PCB-bound domain. Because the absorbance of chlorophyll d is red-shifted compared with that of chlorophyll a, the BV-bound AM1-1557 may be a physiologically relevant feature of A. marina and is potentially useful as an optogenetic switch and/or fluorescence imager.

AB - Cyanobacteriochromes (CBCRs) are linear tetrapyrrole-binding photoreceptors in cyanobacteria that absorb visible and near-ultraviolet light. CBCRs are divided into two types based on the type of chromophore they contain: phycocyanobilin (PCB) or phycoviolobilin (PVB). PCB-binding CBCRs reversibly photoconvert at relatively long wavelengths, i.e., the blue-to-red region, whereas PVB-binding CBCRs reversibly photoconvert at shorter wavelengths, i.e., the near-ultraviolet to green region. Notably, prior to this report, CBCRs containing biliverdin (BV), which absorbs at longer wavelengths than do PCB and PVB, have not been found. Herein, we report that the typical red/green CBCR AM1-1557 from the chlorophyll d-bearing cyanobacterium Acaryochloris marina can bind BV almost comparable to PCB. This BV-bound holoprotein reversibly photoconverts between a far red light-absorbing form (Pfr, Îλ max = 697 nm) and an orange light-absorbing form (Po, Î λ max = 622 nm). At room temperature, Pfr fluoresces with a maximum at 730 nm. These spectral features are red-shifted by 48∼77 nm compared with those of the PCB-bound domain. Because the absorbance of chlorophyll d is red-shifted compared with that of chlorophyll a, the BV-bound AM1-1557 may be a physiologically relevant feature of A. marina and is potentially useful as an optogenetic switch and/or fluorescence imager.

UR - http://www.scopus.com/inward/record.url?scp=84928712660&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=84928712660&partnerID=8YFLogxK

U2 - 10.1038/srep07950

DO - 10.1038/srep07950

M3 - Article

C2 - 25609645

AN - SCOPUS:84928712660

VL - 5

JO - Scientific Reports

JF - Scientific Reports

SN - 2045-2322

M1 - 7950

ER -