micro bio

• differentiated forms of bacteria that can withstand extremes
• highly resistant to being destroyed
• metabolically inactive
• can germinate in favorable condition

peptidoglycan and has protein layers outside

helps draw the water out which adds to the toughness

(salt) binds to water, reduces availability for being a solvent

• Small Acid Soluble Protein;
• binds to DNA and converts it to a more compact and UV resistant form (A-form)

made of protein and provides chemical resistance

• 1. DNA replicates (rod shaped elongates)
• 2. Proteins bind to DNA and segregate it to the poles 
• 3. Formation of the division septum
• 4. Cell separates into 2 cell components and cell wall follows and fills in.

• bacillus + clostridium 
• soil + dwelling

periods of low nutrients or other poor growth conditions

survival and dispersion

remain dominant

protectin

rod shape and gram +

heat resistance, less solvent to carry toxic chemical

fluorescence

cell membrane envaginates cell wall synthesized

mitosis

asymmetrically

genome

• 1. septum formed
• 2. mother cell engulfs forespore
• 3. maturation begins
• 4. cortex forms
• 5. protein coat is built
• 6. loss of water
• 7. mother cell lyses and spore is resealed.

on end

around

both ends

multiple ends

can go back and forth

cell can stop, reorient and then continue allowing it to go in any direction

protein subunits

proton motive force

twitching

corkscrew

at the end of the flagella

are bundled together

are pushed apart

• movement across a solid surface
• no flagella
• uses a protein force

• attraction or repulsion due to a chemical 
• can cause medium before and after run, adjusting size of run (according to distance from attractant)

random movement

attractant = light

relative to an oxygen concentration

relative to density

energy cells have in a certain light do not move in the dark

• carbs, proteins, lipids, nucleic acids
• 50% of dry weight of a cell

• protein and nucleic acid
• informational molecules 
• needed for production of amino acids (proteins) nitrogenous bases (nucleic acids) and peptidoglycan (polysaccharides)

• nucleic acids, phospholipids
• energy conservation molecules

some amino acids and vitamins

enzyme synthesis

• stabilizes negatively charged molecules 
• (protein, membrane and nucleic acid)
• for some enzyme activities

may be needed for cell wall stabilization and sporulation

neeeded in small amounts

• scarce
• needed by most microbes (some found a way to get around needing it)

binds to iron in order to bring it into microbe

• combines with ferric (oxidized) iron and brings it into the cell
• reduces it to ferrous iron

• can bind ferric iron outside of the cell and bring it into the microbe
• found in enteric bacteria (gut)

• not free floating 
• bound to membrane via hydrophobic tail 
• brings in the ferric form and reduces it
• found in marine organisms

• ferric
• insoluble (not capable of being dissolved)

• ferrous 
• soluble

• energy yielding reaction (break down energy source) 
• 1. phototrophic reaction (light)
• 2. chemotrophic reactions (chemical) 
• 3. oxidation of complex substrates

• energy requiring reaction (require energy to work in a cell)
• building the structures required for growth
• reduction steps

exact chemical composition and amounts KNOWN 

• unsure of the relative amounts of nutrients 
• easy to make
• cheaper
• EX: blood agar

• prevent things you dont want
• encourages things you do want

rich, EVERYTHING grows

visible difference between organisms

organisms on surface can isolate individual colonies

• can change concentration
• centrifuge

take trace amounts of each and makes a solution needed for growth

simplest defined minimal amount you can give to an organism and still grow

• contains bile salt and crystal violet to inhibit other bacteria
• contains lactose and pH indicator to differentiate lactose fermenters

• contains Eosin Y (inhibits gram +) and methylene blue as well as lactose 
• E.coli forms a metallic sheen (gloss) due to high lactose fermentation

energy released from a reaction that can be used to do work

• delta G0' (-)
• favorable reaction
• releases energy
• catabolism

• Delta G0' (+) 
• unfavorable reaction
• requires energy

standard conditions

actual/natural conditions

• proteins that lower activation energy for a reaction
• catalysts: speed up reaction
• specific (3D polypeptide structure)
• not consumed in reaction
• does NOT change bioenergetics (free E that can result) of the reaction

active sites

• bound to enzyme
• non-peptide 
• tightly bound as part of the enzyme complex
• covalently linked to peptide
• EX: heme group

• loosely bound to emzyme
• assist in reaction
• non-peptide
• may associate with several different enzymes 
• most derived from vitamins 
• EX: NAD+/NADH

one molecule is reduced, one is oxidized

• gets reduced
• gains electrons (H)
• acceptor

• gets oxidized
• loses electron (H)
• donor

• want to be oxidized
• good DONORS

better electron acceptor

electron carries

electron donor

electron acceptor

main carrier/ currency of energy

anhydride bonds

• 1. glycogen (polyglucose-polysaccharides)
• 2. poly-B-hydroxybutyrate (lipid)
• 3. sulfer polymers-inorganic molecues used by sulfer
• 4. chemolithotrophs

energy rich phosphate or sulfer bonds

longterm storage of energy

ATP

• 1.ATP generate at specific reaction steps
• 2.fermentation mechanism
• 3.can give up phosphate to change ADP to ATP (phosphate transfer)

• 1.ATP generated via proton motive force
• 2.respiratory mechanism 
• 3.required cytoplasmic membrane participation (membrane divides protons and electrons)
• 4. generates proton gradient

used in phototrophs (similar to oxidative phosphorylation)

• 1. nets 2 ATP
• 2. ATP forms through substrate level phosphorylation
• 3. not the most efficient (carbon is not completely oxidized)

• membrane bound
• binds NADH
• transfer 2e- and 2H flavoproteins

• derived from riboflavin
• accepts 2e- and 2H+ from NADH dehydrogenase
• donates 2e- to next carrier

• non-heme iron proteins
• only carries electrons
• contains Fe-S clusters coordinated by cysteines in protein 
• reduction potentials vary from protein to protein

• heme prosthetic groups/iron center
• 1e- in 
• 1e- out (single electron transfer)
• several classes with varying reduction potentials

• hydrophobic (found in membrane) NON-PROTEIN 
• accepts 2e- and 2H+ from prvious carrier
• donates 2e- to next carrier

• uses energy from electrons to pump hydrogen ions out of the cell, creating a gradient across the membrane 
• protons flow from high to low concentrations 
• concentration through ATP aynthase, phosphorulating 
• ADP to ATP

protons that rush through ATPase cause a rotary force of the complex to generate ATP

use of oxygen as the terminal electron acceptor

from organic substrate to terminal electron acceptor with concomitant extrusion of protons across membrane

of organic substrate to form CO2

• discrete transfer steps help conserve energy throughout oxidation
• electron transport allow for separation of protons from electrons

PROTONS to the outside (accumulation of OH- inside)

do work in the cell

• block electron transport, preventing the establishment of a proton gradient 
• EX: carbon monoxide and cyanide 

• allow protons to pass across the membrane (by making them leaky) bypassing the use of ATPase
• EX: dinitrophenol

• uses products of glycolysis (pyruvate) to obtain electron carriers NADH and FADH
• VERY efficient

• 6 CO2
• 3 NADH
• 1 FADH2
• 1 NADPH
• 1 GTP

carry 2e- into electron transport chain

completely oxidized

respiration

using something other than oxygen as terminal electron acceptor

electrons start on reduced inorganic compounds (NOT carbon)

• light excites the electrons
• photosynthesis (aerobic/anerobic)

carbon from CO2

• carbon from organic compounds 
• intermediate carbon compound not oxidized to get energy

• anerobic respiration 
• chemolithotrophy 
• phototrophy
• ALL SEND ELECTRONS TO ELECTRON TRANSPORT CHAIN/ PROTON MOTIVE FORCE TO MAKE ATP