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The colors of different bloods in animalia! ! JesĂşs Maldonado! BIO 361T!

What Causes Blood Color! •  In humans,  we  carry  a  Heme   prosthe3c  group  bound  within  a   globin  protein   •  Fe  (purple)  coordinates  the  binding  of   oxygen   •  Aroma3c  structures  (in  this  case,   nitrogen  heterocycles  and  poryphryin   por3on)    form  a  conjugated  system   [connected  p  orbitals]  can  absorb   certain  wavelengths,  and  reflect   others.   •  In  heme,  high-­‐energy  wavelengths  are   absorbed  (blue)  and  low-­‐energy   wavelengths  (red)  are  reflected.  Only   ferrous  iron  (Fe(II))  binds  to  the  Heme   moiety.     Heme  Prosthe3c  Group  is  Used  in  All  Vertebrate   Groups  with  One  Excep3on  (later)   hLp:// 5/52/Heme_B_anion_3D_ball.png  

Color Changes  Based  on  What  Binds  to   the  Chromophore  

Nothing Bound  

Nitric Oxide   The  color  changes  because   a.)  the  molecule  changes  conforma3on   b.)  electrons  are  in  a  different  arrangement  and  energy  state   c.)  therefore,  the  electrons  absorb  and  reflect  different   wavelengths  

Michael K  Chan,  Recent  advances  in  heme-­‐protein  sensors,  Current  Opinion  in  Chemical  Biology,  Volume  5,  Issue  2,  1  April  2001,  Pages  216-­‐222.  


Hemerythrin Protein  

Sipuncula Worms  

Found in  marine  invertebrates   (sipunculids  (worms),   priapulids  (worms),   brachiopods  (mollusk-­‐like))     Binds  Oxygen       Colorless  to  Light  Violet   transi3on  upon  binding  oxygen    

hLp://­‐ Sipuncula.jpg

Two Fe   Binds  O2  as  a   peroxide   NOT  HEME     Stenkamp,  R.E.  Dioxygen  and  hemerythin.  Chem.  Rev.  1994,  94,  715-­‐728  


Directly Suspended  in  the   Hemolymph  of  Cancer  productus   crab    

Arthropods and  Mollusks     Two  Cu  (I-­‐>II)  ions  and  six  H   coordinate  binding     Colorless  to  blue/purple            


Rehm et  al.  The  diversity  and  evolu3on  of  chelicerate  hemocyanins   BMC  Evolu2onary  Biology  2012,  12,  19.    

Erythrocruorin GIANT  hemoglobins  (144  globins…)     Found  in  segmented  worms     Not  sure  if  it  leads  to  a  different  color      


Vanabin Found  in  sea  squirts,  ascidians,  and   tunicates       May  not  carry  oxygen?     Vanadium  binding  protein.     Dyes  blood  apple-­‐green,  or  blue  or  orange   depending  on  which  vanadium  oxide  it   binds      

hLp:// %29_and_Polycarpa_aurata_%28Sea_quirt%29.jpg

Ernest Baldwin,  An  Introduc2on  to  Compara2ve  Biochemistry;   (Cambridge  University  Press,  Cambridge;  1964).  4th  Edi3on.    

Blue Blood!  

hLp:// puphemutantdragon.files.wordpr­‐blood.jpg

Chlorocruorin Found  in  annelids     (Green  when  dilute,  red  when   concentrated!)     Fox,  H.M.  On  Chlorocruorin   and  Haemoglobin.  Proc.  R.  Soc.   Lond.  B  19  October  1949  vol.   136  no.  884  378-­‐388             Similar  to  heme,   except  methylene   moiety  is  replaced  by   carboxyl  group  

Christmas Tree   Worms   hLp://

Pinnaglobin Found  only  in  one  species  Pinna   squamosa       Manganese-­‐based  poryphyrin1     Clear,  colorless  to  brown  when   oxygenated.       No  one  has  solved  the  crystal   structure  of  the  protein.  (Checked   pdb)   Pinna  squamosa  is  a  clam.  It  gives  brown   pearls.     hLp://    

Respiratory proteids:  researches  in  biological  chemistry.    Chapter  IV.  

Coboglobins: Synthe3c  Globins   Cobalt-­‐subs3tuted  in  hemoglobin   –  Made  to  elucidate  the  role  metals  have  in  the   binding  process  

•  Blood would  be  amber  yellow  (deoxygenated)   to  clear  (oxygenated)   •  Weird,  huh?   • 

B. M.  Hoffman,  D.  H.  Petering.  Coboglobins:  Oxygen-­‐Carrying  Cobalt-­‐Recons3tuted  Hemoglobin  and  Myoglobin.  Proceedings  of  the  Na2onal  Academy  of  Sciences  of   the  United  States  of  America,  Vol.  67,  No.  2  (Oct.  15,  1970),  pp.  637–643  

How about  no  globins?   The  Crocodile  Icefish   (Antar3ca,  below,  -­‐1.9  °C)  has   no  blood.  No  hemoglobin.  No   myoglobin.     Pale  Yellow  blood     They  can  live  because   solubility  of  oxygen  in   seawater  is  inversely   propor3onal  to  T.  Weird   adap3ons  too:         Sidell,  B.  D.  and  O’Brien,  K.M.  When  bad  things  happen  to  good   fish:  the  loss  of  hemoglobin  and  myoglobin  expression  in  Antarc?c   icefishes.  J  Exp  Biol    2006,  209,  1791-­‐1802.        

Drama3c Structural  Changes  Cause  the   Fish  to  Adapt  

Spongy hearts,  increased  mitochondrial  density  

Icefish Re3na   has   extensive   branches  

But, like,  why?   •  Adap3ons   –  Animals  in  low-­‐oxygen  environments  benefit  from   a  low-­‐binding  protein;  oxygen  can  be  dropped  off   easily.  

•  My idea  is  that  different  adap3ons,  occur,  and     color  is  a  byproduct.  

References •  Chromophores/Blood  Color   –  hLp://   –  hLp://­‐is-­‐a-­‐ chromophore.htm#did-­‐you-­‐know  

Blood Color  

Bloods from different animals have different colors

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