导图社区 Coenzymes(psuedoscince naming)
这是一篇关于Coenzymes(psuedoscince naming)的思维导图,主要内容有coreactant phospate carriers、coreactant hydride ion e- carriers、prosthetic e- transfer groups、defination等。
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Coenzymes(psuedoscince naming)
coreactant phospate carriers
Adanine+Guanosine
ATP,ADP,AMP
GTP,GDP,GMP
reactions catalysts
phosphorylation
many kinases
often very spontaneous, ATP has very high energy structure.
columbic repulsive forces between neighboring negative charged phosphates
it self undergoes
hydrolysis
resupplemented by oxidative phosphorylation/photophosphorylation
coreactant hydride ion e- carriers
Nicotinamide adenine dinucleotides
oxidated state
NAD+
NADP+
final electrons acceptor in photophosphorylation
reducted state
NADH
electron donator in oxidative phosphorylation
NADPH
supplies electrons for anabolic reactions
access enzyme class
Nicotinamide nucleotide-linked dehydrogenase
reversible reactions
binding
loose, noncovalent
should be considered as reactant
reduction potential
independent of enzymes
reaction catalysts
Oxidation
accepts a hydride ion H:-
Reduction
donates a hydride ion H:-
Strong reducing potential
prosthetic e- transfer groups
direct e- carriers
as in reduction of Fe3+---Fe2+
cytochromes(proteins)
a-type cytochromes
Heme A(prosthetic group)
noncovalent interaction
b-type cytochromes
Iron protoporphyrin IX
c-type cytochromes
Heme C
covalent attachment
distinguish
light absorbtion spectra
a~600nm
b~560nm
c~550nm
most integral membrane proteins
exept cytochrome c: periphral protein through electrostatic interaction
Ion-sulfur centers
1 Fe sulfur center
2 Fe 2S sulfur center
4 Fe 4S sufur center
Rieske iron-sulfur protein
S in cys residues
all requires 4 sulfur in cys residues for stabalization
exept the rieske one stabalized by His
hydride ion 2 e- carriers
hydrogen atom 1 e- carriers
hydrophobic quinone
coenzyme Q
Ubiquinone(Q)
fully oxidized
Semiquinone radical(.QH)
Ubiquinol(QH2)
fully reduced
chloroquinone
plastoquinone
lipid soloble
move freely in hydrophobic membrane region
Flavin nucleotides
FADH2
electrons donator in respiratory ETC
FADH
FAD+
access proteins
Flavoproteins
tight bonding, sometimes covalent
should be considered as part of active site (prosthetic group)
protein dependent
e- transfer
can transfer either 1 or 2 e-
defination
prosthetic group
A metal ion or an organic compound (other than amino acids) that is covalently bound to a protein and is essential to its activity
it's reduction potential dependent on microenviroment of binded proteins
the reaction goes into direction of increasing reduction potential
reducing equivalent
a single electron equivalent transferred in an oxidation-reduction reaction
remove two hydrogen atoms on substrate
release one as proton and itself accept a hydride ion H:-
seperate pools in cell for NADPH and NADH with different redox potentials
[reduced form]/[oxidized form]
relative high for NADPH
more reduced form to catalyst anabolic reductions
relative low for NADH
more oxidized form to catalyst the metabolism oxidation