Difference between revisions of "Part:BBa K1640020"

Revision as of 03:43, 15 September 2015

psbA

n/a

Usage and Biology: PsbA encodes the Photosystem II reaction centre subunit D1. This product forms a heterodimer with D2, encoded by psbD, to form the Photosystem II reaction centre (Marder, Chapman, Telfer, Nixon, & Barber, 1987). The primary function of the D1/D2 reaction centre complex is to transfer electrons from the chlorophyll P680 to two quinones, designated QA and QB. To this end, D1 has functions both at the oxidation and reduction stages of the reaction.

D1 accepts electrons from P680, transferring it to QB. A tyrosine of D1 reduces the resulting P680 cation, resulting in a tyrosine radical. This radical acts as an oxidising agent for the oxidation of water through the oxygen evolving complex (OEC) of PSII (Ferreira, Iverson, Maghlaoui, Barber, & Iwata, 2004). In addition, this protein is vital to the assembly of both the OEC and QB within PSII. Site-directed mutagenesis studies have revealed an aspartate residue of D1 to be both structurally coupled to and involved in the assembly of the Mn cluster within the OEC (Chu, Debus, & Babcock, 2001; Nixon & Diner, 1992). Similarly, inhibition studies involving the binding of herbicides to D1 have revealed this protein to contain a niche for the binding of QB (Erickson et al., 1989; Jansen, Mattoo, Malkin, & Edelman, 1993).

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 __NOTOC__
 <partinfo>BBa_K1640020 short</partinfo>
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-<!-- Add more about the biology of this part here
+Usage and Biology:
-===Usage and Biology===
+PsbA encodes the Photosystem II reaction centre subunit D1. This product forms a heterodimer with D2, encoded by psbD, to form the Photosystem II reaction centre (Marder, Chapman, Telfer, Nixon, & Barber, 1987). The primary function of the D1/D2 reaction centre complex is to transfer electrons from the chlorophyll P680 to two quinones, designated QA and QB. To this end, D1 has functions both at the oxidation and reduction stages of the reaction.
+D1 accepts electrons from P680, transferring it to QB. A tyrosine of D1 reduces the resulting P680 cation, resulting in a tyrosine radical. This radical acts as an oxidising agent for the oxidation of water through the oxygen evolving complex (OEC) of PSII (Ferreira, Iverson, Maghlaoui, Barber, & Iwata, 2004). In addition, this protein is vital to the assembly of both the OEC and QB within PSII. Site-directed mutagenesis studies have revealed an aspartate residue of D1 to be both structurally coupled to and involved in the assembly of the Mn cluster within the OEC (Chu, Debus, & Babcock, 2001; Nixon & Diner, 1992). Similarly, inhibition studies involving the binding of herbicides to D1 have revealed this protein to contain a niche for the binding of QB (Erickson et al., 1989; Jansen, Mattoo, Malkin, & Edelman, 1993).
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