Abstract
This chapter discusseses PS I in detail. Chlamydomonas has been an incredibly powerful and productive platform from which to study PS I. PS I is composed of 14 polypeptides and its core cofactors are explained in depth. Energy transfers within, from PS I and to other cell is also elaborated. After a shift of the mutant to the nonpermissive temperature, PS I remained stable, indicating that the effect was upon assembly. PS I can be thought of as a light-driven electron pump, transferring electrons from plastocyanin (or cytochrome c 6) on the lumenal side to ferredoxin on the stromal side, both across the thylakoid membrane and over an energy barrier. PS I can function as part of the linear or cyclic electron transport pathways. The resemblance of PS I from this organism to that of higher plants also allows the study of questions that would not be easy or possible in either plants or cyanobacteria. These include: the mechanisms by which external antenna proteins attach to the PS I, and how these interactions are regulated; the structural arrangement of these antenna proteins with PS I, and how these relate to pathways of excitation quenching; and the role of specialized membrane domains in the function of PS I.
| Original language | English (US) |
|---|---|
| Title of host publication | The Chlamydomonas Sourcebook 3-Vol set |
| Publisher | Elsevier Inc. |
| Pages | 541-572 |
| Number of pages | 32 |
| Volume | 2 |
| ISBN (Print) | 9780123708731 |
| DOIs | |
| State | Published - 2009 |
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ASJC Scopus subject areas
- Agricultural and Biological Sciences(all)
Cite this
Photosystem I. / Redding, Kevin.
The Chlamydomonas Sourcebook 3-Vol set. Vol. 2 Elsevier Inc., 2009. p. 541-572.Research output: Chapter in Book/Report/Conference proceeding › Chapter
}
TY - CHAP
T1 - Photosystem I
AU - Redding, Kevin
PY - 2009
Y1 - 2009
N2 - This chapter discusseses PS I in detail. Chlamydomonas has been an incredibly powerful and productive platform from which to study PS I. PS I is composed of 14 polypeptides and its core cofactors are explained in depth. Energy transfers within, from PS I and to other cell is also elaborated. After a shift of the mutant to the nonpermissive temperature, PS I remained stable, indicating that the effect was upon assembly. PS I can be thought of as a light-driven electron pump, transferring electrons from plastocyanin (or cytochrome c 6) on the lumenal side to ferredoxin on the stromal side, both across the thylakoid membrane and over an energy barrier. PS I can function as part of the linear or cyclic electron transport pathways. The resemblance of PS I from this organism to that of higher plants also allows the study of questions that would not be easy or possible in either plants or cyanobacteria. These include: the mechanisms by which external antenna proteins attach to the PS I, and how these interactions are regulated; the structural arrangement of these antenna proteins with PS I, and how these relate to pathways of excitation quenching; and the role of specialized membrane domains in the function of PS I.
AB - This chapter discusseses PS I in detail. Chlamydomonas has been an incredibly powerful and productive platform from which to study PS I. PS I is composed of 14 polypeptides and its core cofactors are explained in depth. Energy transfers within, from PS I and to other cell is also elaborated. After a shift of the mutant to the nonpermissive temperature, PS I remained stable, indicating that the effect was upon assembly. PS I can be thought of as a light-driven electron pump, transferring electrons from plastocyanin (or cytochrome c 6) on the lumenal side to ferredoxin on the stromal side, both across the thylakoid membrane and over an energy barrier. PS I can function as part of the linear or cyclic electron transport pathways. The resemblance of PS I from this organism to that of higher plants also allows the study of questions that would not be easy or possible in either plants or cyanobacteria. These include: the mechanisms by which external antenna proteins attach to the PS I, and how these interactions are regulated; the structural arrangement of these antenna proteins with PS I, and how these relate to pathways of excitation quenching; and the role of specialized membrane domains in the function of PS I.
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U2 - 10.1016/B978-0-12-370873-1.00023-X
DO - 10.1016/B978-0-12-370873-1.00023-X
M3 - Chapter
AN - SCOPUS:78650239460
SN - 9780123708731
VL - 2
SP - 541
EP - 572
BT - The Chlamydomonas Sourcebook 3-Vol set
PB - Elsevier Inc.
ER -