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Metabolism
all biochemical process to life
Catabolism
breaking down big molecules (protein, carbs, lipids, fats) into smaller parts (ATP, reducing power, precursor metabolites)
Anabolism
using small molecules (ATP, reducing power, precursors) and nutrients (CHNOPS) to make larger components (flagella, organelles)
Energy
capacity to do work
Photo
light energy
Chemo
chemical energy
Litho
inorganic electrons
Organo
organic electrons
Auto
CO2 as carbon source
Hetero
organic carbon
Energy sources
light (photosynthesis), dark (ATP, reducing power), chemical (respiration, fermentation)
Chemical energy
respiration and fermentation
Three types of work
chemical, transport, and mechanical
Chemical work
polymerization of small precursor molecules for synthesis of complex molecules (amino acids -> proteins)
Transport work
move molecules against gradient (ATP)
Mechanical energy
rotate flagella for motility
ATP is stood for
adenosine tri-phosphate
ATP function
primary molecule used to conserve the energy supplied by an energy source
ATP components
adenine, ribose, and 3 phosphate groups
Oxidation
loss of electron
Reduction
gain electron
Reducing agent
molecule that donates electrons (reducing power)
Oxidizing agent
molecule that accepts electrons
Standard reduction potential
measure of the tendency of reducing agent to donate electron
Good electron donators
NADH/NADPH cus they're more electronegative
Reducing power molecules
NADH, FADH, NADPH
NADH
donate electrons to ETC and to NADPH
NADPH
donates electrons to other molecules
Electron transport chain
electrons flow from electron carrier having the most negative reduction potential to the most positive carrier
Electron carriers
direct electrons to electron acceptor, the are close together to prevent energy loss
Enzyme
protein catalysts that have great specificity for substrates
Catalyst
increase rate of reaction without being used up in process
Enzyme structure
proteins and the apoenzyme and cofactor (holoenzyme)
Apoenzyme
protein in enzyme
Cofactor
non-protein in enzyme
Holoenzyme
apoenzyme + cofactor
Prosthetic group
cofactor firmly attached to apoenzyme
Coenzyme
cofactor loosely attached to apoenzyme
Enzyme kinetics
enzyme is specific for substrate, coenzyme picks chemical group from substrate 1 and attaches it to substrate 2, substrates are released from enzyme
Enzyme environmental effects
amount of substrate present, temp, and pH
Amount of substrate present
low conc or high conc of substrate
What happens when there is a low concentration of substrate for enzymes
hard for enzyme to find substrates, slow velocity
What happens when there is a high concentration of substrate for enzymes
easy for enzyme to find substrate, fast velocity
What happens when temp is high for enzymes
denatures proteins
What happens if pH is too high or too low
enzyme slows or speeds up
Enzyme regulation
synthesis of enzyme, pre-existing enzymes/post translational, and feedback inhibition
Synthesis of enzyme
rate of transcription or translation (gene expression) to control amount of enzymes
pre-existing/post translational enzymes regulation
already made enzymes go through allosteric regulation and covalent modification
Allosteric regulation
effector binds reversibly to regulatory site and causes conf. Change of enzyme, can increase or decrease enzyme activity through positive and negative effectors
Covalent modification
addition/removal of particular chemical group
Feedback inhibition
use pacemaker enzyme to catalyze the rate-limiting (slowest) reaction in pathway, ensures balance (supply/demand)